Semenogelin I Recombinant Protein Antigen Summary
Description |
A recombinant protein antigen with a N-terminal His6-ABP tag corresponding to human SEMG1. Source: E. coli
Amino Acid Sequence: APNPKQEPWHGENAKGESGQSTNRE Fusion Tag: N-terminal His6ABP (ABP = Albumin Binding Protein derived from Streptococcal Protein G)
This product is intended to be used as a blocking antigen for antibody competition assays. Any other use of this antigen is done at the risk of the user. The use of this product for commercial production is strictly prohibited. Please contact technical support if you have any questions. |
Source |
E. coli |
Protein/Peptide Type |
Recombinant Protein Antigen |
Gene |
SEMG1 |
Purity |
>80% by SDS-PAGE and Coomassie blue staining |
Applications/Dilutions
Dilutions |
- Antibody Competition 10-100 molar excess
|
Application Notes |
This recombinant antigen is only intended to be used as a blocking agent to confirm antibody specificity with the corresponding antibody, catalog number NBP2-62646. It is purified by IMAC chromatography, and the expected concentration is greater than 0.5 mg/ml. For current lot information, including availability, please contact our technical support team click nb-technical@bio-techne.com |
Theoretical MW |
20 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Packaging, Storage & Formulations
Storage |
Store at -20C. Avoid freeze-thaw cycles. |
Buffer |
PBS and 1M Urea, pH 7.4. |
Preservative |
No Preservative |
Purity |
>80% by SDS-PAGE and Coomassie blue staining |
Alternate Names for Semenogelin I Recombinant Protein Antigen
Background
Semenogelin I (SgI) and Semenogelin II (SgII) are the major seminal vesicle secreted proteins in human semen (reviewed in Lundwall, 2002 and Bonilha et al, 2006). SgI and SgII, in semen both originate from the glandular epithelium of the seminal vesicles which secrete them at high concentrations. SgII is also secreted by the epididymis at lower concentrations. SgI and SgII interact both non-covalently and covalently by disulphide bridges to instantly form a gel-like coagulum upon ejaculation. Fibronectin is also a key component of the coagulum. The gel structure dissolves spontaneously within minutes after ejaculation as a result of proteolytic degradation of SgI/SgII by prostatic serine protease (PSA) and other proteases which cleave SgI/SgII into fragments. The high concentration of SgI/SgII in human semen led to the concept of SgI/SgII as a potentially useful marker for semen identification (reviewed in Pang and Cheung, 2006). Whereas SgI/SgII were originally identified as the major components present in seminal vesicle secretion, they are now known to be expressed in a number of tissues. The list includes seminal vesicles, epididymis, vas deferens, prostate, skeletal muscle, kidney, colon, trachea, lung, breast and retina as well as in several malignant tissues and cell lines (reviewed in Lundwall, 2002 and Bonilha et al, 2006). The non-genital expression of SgI/SgII suggests that these proteins also have functions that are unrelated to sperm. Human Sg1 is a non-glycosylated protein of 439 amino acids with a molecular weight of approx. 50 kDa. A few percent of the worlds population also carry an allele that gives rise to a truncated SgI molecule with a molecular mass of 43 kDa. Human SgII is a 559 amino acid protein with a molecular weight of approx. 63 kDa. SgII has a potential site for N-linked glycosylation and approximately half of the molecules in human semen are glycosylated yielding two SgII species with a different of 5 kDa. SgI has a single Cys residue and SgII has two Cys residues, and the molecules can exist as covalent homo- and heteromultimers.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are
guaranteed for 3 months from date of receipt.
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