SRP72 Antibodies

Signal recognition particle subunit SRP72 (SRP72)

Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. Binds the 7S RNA only in presence of SRP68.

This ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function. .

Gene Information

Human
Gene Name:	SRP72
Uniprot:	O76094
Entrez:	6731

Family

Belongs to:
SRP72 family

Alternative Names

signal recognition particle 72kDa

Molecular Weight

Mass (kDA):
74.606 kDA

Genomic Context

Human
Location:	4q12
Sequence:	4; NC_000004.12 (56467617..56503681)

Subcellular Localizations

Cytoplasm. Endoplasmic reticulum.

Diseases

• Familial Hypocalciuric Hypercalcaemia
• Malignant Neoplasms
• Neoplasm Metastasis
• Dermatomyositis
• Rheumatism
• Neoplasms
• Murine Hepatitis
• Malignant Neoplasm Of Breast
• Malignant Neoplasm Of Liver
• Pancytopenia
• Malignant Neoplasm Of Lung
• Carcinoma

• Myopathy
• Acute Erythroblastic Leukemia
• Primary Effusion Lymphoma
• Nervousness
• Pituitary Diseases
• Sudden Death
• Aplastic Anemia

Pathways

• Transport
• Protein Targeting
• Translation
• Nuclear Export
• Protein Transport
• Localization
• Methylation
• Cell Death
• Cell Growth
• Secretion
• Transposition
• Programmed Cell Death
• Complement Activation

• Ribosome Assembly
• Cell Cycle
• Rna Folding
• Protein Import
• Secretory Pathway
• Cell Proliferation
• Induction Of Apoptosis

PTMs

• Cleavage
• Phosphorylation

• Glycosylation
• Methylation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/SRP72

Best Uses Of The SRP72 Marker

The SRP72 protein has many functions in cell biology. In addition to being a subunit of signal recognition particles, it is involved in alternative mRNA splicing. In this article, you'll learn more about SRP72, how it is used in cell biology, and what methods it can be used with. Boster Bio has high-affinity primary antibodies that are trusted by the research community. These antibodies are validated for use in Western Blotting, Immunohistochemistry, and ELISA.

Protein transfer efficiency by membrane staining

The Boster Bio protein transfer efficiency by membrane stasing method has been able to capture the binding efficiency of antibodies to specific proteins with the highest sensitivity. This method allows users to analyze the transfer efficiency of multiple proteins to one membrane. This method can save considerable time when compared to the traditional Western blotting. The PVDF membrane offers enhanced re-probing capacity as compared to the NC membrane.

Protein quantification is a common requirement for many researchers. Boster Bio offers custom Western blotting services including extraction of total proteins from tissues and construction of premade blots. It is also capable of immunostaining blots with any antibodies. Once immunostaining is done, the Boster Bio team will analyze the results and send you high quality digital images for further analysis.

The protein transfer efficiency by membrane staining by Boster Bio is greatly enhanced when using the high-quality gels with high-quality electrophoresis reagents. However, this technique is not suited for all kinds of experiments. Because the gels are very thick, the protein must migrate further to reach the membrane. A thicker gel is also less efficient because the proteins are removed from the gel matrix.

The high-sensitivity ELISA platform Picokine(tm) enhances detection sensitivity to picogram levels. Picokine ELISA kits have been validated for a wide range of samples and are available for download. Moreover, they have a polymer-based secondary antibody Supervision, which saves you up to 30 minutes of IHC. In addition to these excellent options, Boster Bio also provides high-quality reagents and technical support from BeNeLux distributor Sanbio.

The Boster Bio protein transfer efficiency by membrane stasing method also allows for the visualisation of proteins in the gels. This helps in assessing the uniformity of migration of proteins. Coomassie stain and copper staining are both useful for checking the transfer efficiency. Membrane staining also helps in observing the results of SDS-PAGE separation. These results are similar to those obtained by the standard western blotting method.

A pooled human serum sample containing 10 mg of protein was resolved by 10% SDS-PAGE and transferred to PVDF or nitrocellulose membranes. Membranes were stained with Coomassie Brilliant Blue. Following this, the membranes were stained with 50% methanol/water at 0 degC. Finally, quantification of the bands using Image Lab software was performed. The results are presented in the graph below.

Membrane staining with DB-71 is a reliable method of measuring protein transfer efficiency. It is less prone to membrane failure compared to other methods. Wet transfer is the preferred method when protein is large and needs to be purified. The gel and membrane are sandwiched between absorbent materials and clamped between solid supports. This procedure is more efficient and consistent than the other two methods but is more time-consuming. The sandwich also contains bubbles, which can contaminate the proteins.

Function of SRP72 in alternative pre-mRNA splicing

The alternative splicing of pre-mRNA is central to the generation of diversity in metazoan genomes. This process involves recognition of both constitutive and alternatively spliced exons by cis-regulatory elements and includes the exons from both of these types in the pre-mRNA. Alternative splicing occurs based on the competitive binding of splicing factors.

The role of SRP72 in alternative splicing is thought to be involved in the regulation of post-transcriptional gene expression. It also functions in nuclear export of mRNA and regulates the initiation of mRNA translation and degradation. This protein binds to the eukaryotic initiation factor 4E binding protein and promotes cap-dependent translation of specific mRNAs. SRSF6 has additional functions outside of mRNA processing. In neuroblastoma cells, it regulates the apoptotic pathway.

Nutrients play a crucial role in controlling the alternative splicing of pre-mRNA. Some nutrients directly affect the events of pre-mRNA splicing while others act indirectly through pancreatic hormones. Signaling pathways downstream of nutrients, metabolites, and hormones are important for regulating alternative splicing. A nutrient-regulated diet may improve health by promoting healthy splicing.

Using a transient expression system, a functional clone of SRP72 has been identified. The cloned RNA has a unique 80-nucleotide sequence that can be targeted for degradation. Furthermore, knockdown of BC200 results in an increase of apoptosis in ten different cell lines. Furthermore, it has been shown that BC200 can bind SRP9, SRP14, and RNA-binding proteins. These interactions were verified through mass spectrometry and polysome profiling experiments.

Another study found that a vitamin E-deficient diet decreases the expression of splicing factors in the liver. Vitamin E-deficient diets inhibit the splicing of SC35 and other splicing factors. This suggests that these foods are important for proper gene expression. They may also inhibit insulin signaling in the liver. However, the findings from this study suggest that dietary PUFAs have a role in regulating gene expression.

A ribonucleoprotein complex called the signal recognition particle (SRP) mediates co-translational protein targeting to the endoplasmic reticulum. The SRP complex binds the signal sequence of a nascent protein and directs it to an ER-anchored SRP receptor. The ribosome-nascent chain complex is transported to the SR and mature snRNPs accumulate in nucleoplasmic splicing speckles. The biogenesis of U6 occurs in the nucleus.

The H/ACA snoRNAs contain cryptic exons, which generate stop codons and frameshift mutations that affect the resulting protein. The C/D box snoRNAs, on the other hand, are less structured, consisting of a loose hairpin with a noncanonical kink-turn motif. The H/ACA snoRNAs are enriched in guide sequences.

Application of SRP72 as a signal recognition particle subunit

Antibodies against SRP72 are used in many biological assays and are known to react with a variety of animal samples. The Boster Bio team used mouse and rabbit samples to generate antibodies against SRP72. Signal-recognition-particle assembly plays a crucial role in targeting proteins. The ribonucleoprotein complex may also interact with a docking protein in the ER membrane and participate in elongation arrest functions.

The polypeptide of the present invention has been purified using a peptide spectrometry method. It can be directly injected into in-vivo tissues or externally transferred by using a carrier containing a virus, phage, or plasmid. After purification, the polynucleotide should begin to collect its first peak before washing out.

The polypeptide express spectrum of the present invention is consistent with that of human SRP. The two proteins perform the same biological function and control secretory protein transposition, which occurs during the apoptosis process. If the level of SRP72 in a cell is abnormal, it may result in an atypical dying process, or relevant disease. Thus, SRP72 is a valuable tool for the treatment of disease.

Autoantibodies present in the serum can serve as useful diagnostic markers and probes for biochemical pathways and signaling. Although the mechanisms underlying the generation of autoantibodies remain elusive, they are a critical missing link in the understanding of rheumatologic diseases. The recent experiments suggest that cell death-specific modifications are responsible for bypassing tolerance to highly conserved autoantigens.

SRP72 is an excellent candidate for use in qRT-PCR. It has numerous advantages over other signal recognition particle subunits. It has several other uses in boster bio. QRT-PCR is a versatile tool for quantitative gene expression analysis. It allows for the measurement of quantity, sensitivity, and linearity. It is also widely used in other diagnostic tests.

The chromatin-bound complex can induce chromatin compaction. In addition to catalyzing monoubiquitylation of histone H2A, the chromatin-bound complex also induces a halting state for Pol-II. Thus, it acts as a signal recognition particle subunit in Boster bio. In this way, SRP72 can provide a useful signal recognition particle for the development of gene therapy therapies.