KHSRP Antibodies

Far upstream element-binding protein 2 (KHSRP)

Binds to the dendritic targeting element and might play a role in mRNA trafficking (By similarity). Part of a ternary complex that binds to the downstream control sequence (DCS) of the pre-mRNA.

Mediates exon inclusion in transcripts that are subject to tissue-specific alternative splicing. May interact with single- stranded DNA in the far-upstream element (FUSE).

Gene Information

Human
Gene Name:	KHSRP
Uniprot:	Q92945
Entrez:	8570

Family

Belongs to:
KHSRP family

Alternative Names

FBP2far upstream element-binding protein 2; FUBP2p75; FUSE binding protein 2; FUSE-binding protein 2; KH type-splicing regulatory protein; KH-type splicing regulatory protein; KSRPMGC99676

Molecular Weight

Mass (kDA):
73.115 kDA

Genomic Context

Human
Location:	19p13.3
Sequence:	19; NC_000019.10 (6413102..6424811, complement)

Tissue Specificity

Detected in neural and non-neural cell lines.

Subcellular Localizations

Nucleus. Cytoplasm. A small proportion is also found in the cytoplasm of neuronal cell bodies and dendrites.

Diseases

• Malignant Neoplasms
• Neoplasms
• Hyperplasia
• Ataxia
• Malignant Neoplasm Of Breast
• Carcinoma
• Hereditary Diseases
• Liver Carcinoma
• Colonic Neoplasms
• Inflammatory Response
• Nervousness
• Infective Disorder
• Neuroblastoma

• Cell Transformation, Neoplastic
• Kidney Failure, Chronic
• Nervous System Disorder
• Kidney Failure
• Virus Diseases
• Autoimmunity
• Malnutrition

Interacting Proteins

• Ywhaz

Pathways

• Localization
• Translation
• Pathogenesis
• Cell Proliferation
• Viral Replication
• Inflammatory Response
• Mrna Stabilization
• Mrna Processing
• Oogenesis
• Secretion
• Transport
• Cell Adhesion
• Cell Activation

• T Cell Activation
• Aging
• Lung Development
• Cell Fate Determination
• Protein Secretion
• Oxidative Phosphorylation
• Regulation Of Type I Interferon Production

PTMs

• Phosphorylation
• Cleavage

• Biotinylation
• Deamination

• Methylation

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

Best Uses Of The KHSRP Marker

This article discusses the methods for detecting protein transfer efficiency using autoradiography film and membrane staining. The methods are applicable to Boster's high-affinity primary antibodies. You can read the article in full by clicking on the following link:

Boster's high-affinity primary antibodies

Recent studies have focused on the role of KHSRP in cancer metastasis. They show that this protein plays multiple roles in invasion and metastasis, and has a strong association with a patient's prognosis. However, this protein may have an opposite role in liver and gastric cancers. For this reason, Boster's high-affinity primary antibodies and the KHSRP marker have important clinical implications.

The protein is highly regulated by genotoxic stress. It is regulated by the MAPK14/MAPKAPK2 signaling module. In fact, KHSRP is highly correlated with X-chromosome-linked intellectual disability (X-Chromosome) and a component of neuronal RNA granules. KHSRP also co-localizes with Dicer and some pre-miRNAs in distal axons of the DRG. Hence, it is involved in orienting decisions at different levels.

Additionally, the deletion of KHSRP affects the levels of Per2 mRNA in adipose tissue and the liver. These findings suggest that KHSRP has a tissue-restricted role in the stability of Per2 mRNA. The study also points to a potential therapeutic role for KHSRP in autoimmune disease. It is hoped that the results of this study will lead to better treatments for autoimmune diseases.

The use of KHSRP as a marker may be useful for determining the role of myomiR during muscle regeneration. Additionally, this marker also promotes mRNA decay. This could be beneficial for the treatment of dystrophic disease. Hence, Boster's high-affinity primary antibodies against KHSRP are a valuable tool for researchers. When it comes to identifying the function of KHSRP, this protein has a major role to play in muscle regeneration.

The KHSRP protein is required for many processes, including cell proliferation. Knocking down KHSRP is beneficial for certain aspects of mice physiology, while overexpression improves cell proliferation. Likewise, KHSRP expression and function must be tightly regulated to maintain normal physiology and to prevent tumors. The expression of KHSRP is tightly regulated and must be finely modulated in order to achieve optimal results.

Polyclonal antibodies are made by immunizing animals with synthetic peptides that are similar to the amino terminus of the human KHSRP protein. These antibodies are then purified using peptide affinity chromatography. They are then used for tissue culture. When using polyclonal antibodies to detect human disease, the process of affinity maturation and off-rate selection can be accelerated to obtain highly specific binders.

Methods for detecting protein transfer efficiency by membrane staining

One way to measure the efficiency of transfer is to stain proteins on the membrane with Ponceau S. The proteins on the membrane are then probed with epitope-specific antibodies or conjugates to determine whether they have transferred properly. The transfer efficiency of a given protein depends on several factors. The amount of Ponceau S needed depends on the size and shape of the proteins, the thickness of the membrane, and the concentration of acrylamide used in the experiment.

Proteins bound to the transfer membrane are useful for various applications. For example, they can be used for marking the locations of molecular weight standards. Three different membrane-staining methods are described in this unit. Detection limits are given for each method along with lists of compatible blot transfer membranes. A support protocol describing alkali treatment is also included. It enables researchers to compare staining patterns directly.

After preparing the blots, protein stains are used to check the transfer efficiency. To determine the transfer efficiency, the blot should contain a lane of standard proteins. Standard proteins are mixtures of purified proteins with known molecular weights. The standard proteins may be unstained or stained with a dye to aid in the analysis of transfer efficiency. Alternatively, standard proteins may be labeled for detection with fluorescence or chemiluminescence.

One method for detecting protein transfer efficiency by membrane stainning is to use reversible dyes. These dyes do not interfere with downstream steps and are used for analyzing protein binding in cell membranes. Another stain-free detection method uses a trihalo compound. The compound binds to tryptophan residues in proteins, causing fluorescence. A CCD camera can detect the fluorescent signal.

The wet transfer method is a common technique that works well for most routine protein work. It can be optimized by using different transfer buffers. Using a proper cooling system allows the transfer of proteins to take place over long periods of time or rapidly at higher voltages. Furthermore, most systems allow multiple gels to be transferred simultaneously. This is an excellent choice for quantitation. In this way, you can compare the transfer efficiency of different proteins in the same gel.

Another way to determine the efficiency of protein transfer by membrane staining is to compare the levels of the primary antibodies to the amounts of proteins transferred by the membrane. Indirect methods are more sensitive than direct detection because multiple secondary antibodies bind to the membrane, amplifying the signal. Furthermore, they are much cheaper. If you plan to perform several experiments, you can always try using FLASHBlot Transfer Buffer.

Detecting protein transfer efficiency by autoradiography film

Detecting protein transfer efficiency by autoradiograph film involves examining the membrane for fluorescence. It is possible to measure the percentage of transferred protein by evaluating its lane-to-lane consistency. Detecting transfer efficiency requires an adequate amount of transfer efficiency. The range of transfer efficiency is between 10 to 70 mg of protein load. To confirm transfer efficiency, a staining gel and membrane are used. This step can be useful for troubleshooting.

Autoradiography is a method for assessing the spatial distribution of radioactive materials within tissues, cells, or molecules. It uses X-ray film to visualize proteins. The main radioisotopes used in autoradiography are 32P and 35S, which are low-energy b-emitters and high-energy c-emitters, respectively. However, other radioisotopes may be used, such as 3H and 14C.

Generally, increasing the amount of protein loaded on a gel or blot results in a plateau. This plateau is caused by multiple layers of the target protein bound to the membrane. As a result, the density of the transfer efficiency decreases with protein load. This is also a problem for autoradiography film. For this reason, cooled CCD camera technologies have emerged. They offer greater dynamic range than film. Also, sophisticated software analysis tools allow accurate densitometric densitometry analysis of western blots.