Recombinant Human Cation Channel Sperm-Associated Protein 1 (CATSPER1) Protein (His)

Beta LifeScience SKU/CAT #: BLC-07529P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Human Cation Channel Sperm-Associated Protein 1 (CATSPER1) Protein (His)

Beta LifeScience SKU/CAT #: BLC-07529P
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Product Overview

Description Recombinant Human Cation Channel Sperm-Associated Protein 1 (CATSPER1) Protein (His) is produced by our Yeast expression system. This is a protein fragment.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb Q8NEC5
Target Symbol CATSPER1
Synonyms (CatSper1)(hCatSper)
Species Homo sapiens (Human)
Expression System Yeast
Tag C-6His
Target Protein Sequence MDQNSVPEKAQNEADTNNADRFFRSHSSPPHHRPGHSRALHHYELHHHGVPHQRGESHHPPEFQDFHDQALSSHVHQSHHHSEARNHGRAHGPTGFGLAPSQGAVPSHRSYGEDYHDELQRDGRRHHDGSQYGGFHQQSDSHYHRGSHHGRPQYLGENLSHYSSGVPHHGEASHHGGSYLPHGPNPYSESFHHSEASHLSGLQHDESQHHQVPHRGWPHHHQVHHHGRSRHHEAHQHGKSPHHGETISPHSSVGSYQRGISDYHSEYHQGDHHPSEYHHGDHPHHTQHHYHQTHRHRDYHQHQDHHGAYHSSYLHGDYVQSTSQLSIPHTSRSLIHDAPGPAASRTGVFPYHVAHPRGSAHSMTRSSSTIRSRVTQMSKKVHTQDISTKHSEDWGKEEGQFQKRKTGRLQRTRKKGHSTNLFQWLWEKLTFLIQGFREMIRNLTQ
Expression Range 1-445aa
Protein Length Partial
Mol. Weight 52.7 kDa
Research Area Others
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Voltage-gated calcium channel that plays a central role in calcium-dependent physiological responses essential for successful fertilization, such as sperm hyperactivation, acrosome reaction and chemotaxis towards the oocyte.
Subcellular Location Cell projection, cilium, flagellum membrane; Multi-pass membrane protein. Note=Specifically located in the principal piece of sperm tail.
Protein Families Cation channel sperm-associated (TC 1.A.1.19) family
Database References

HGNC: 17116

OMIM: 606389

KEGG: hsa:117144

STRING: 9606.ENSP00000309052

UniGene: PMID: 28507119

  • Electrophysiological studies showed a significant increase in Cd(2+) and manganese (Mn(2+)) currents through the CaV3.1 mutants as well as a reduction in the inhibitory effect of Cd(2+) on the Ca(2+) current. PMID: 27134080
  • Sperm with a near absence of CatSper current failed to respond to activation of CatSper by progesterone and there was fertilization failure at IVF. PMID: 26453676
  • The role of CATSPER1 in idiopathic asthenospermia pathogenesis: exonal SNP rs1893316 in CATSPER1 significantly correlated with idiopathic asthenospermia risk PMID: 26354096
  • Sox5 and Sox9 cause a significant increase in transactivation of the Catsper1 promoter. PMID: 25101494
  • Progesterone via CatSper activates the PI3K-AKT pathway required for motility and hyperactivation but not for acrosome reaction. PMID: 23623968
  • The immediate upstream region and the first exon in the human CATSPER1 gene negatively regulate transcriptional activity. PMID: 23313885
  • This work reports the cloning and characterization of the promoter regions in the human and murine Catsper1 genes. The immediate upstream region and the first exon in the human CATSPER1 gene negatively regulate transcriptional activity. The mouse Catsper1 promoter exhibited transcriptional activity in both orientations and displayed significant expression levels in mouse testis in vivo. PMID: 23313885
  • CatSper is indeed the principal Ca2+ channel of human spermatozoa, and that it is strongly potentiated by progesterone. PMID: 23530196
  • CatSper activation can elicit functionally different behaviors according to the sensitivity of the Ca(2+) store, which may be regulated by capacitation and NO from the cumulus. PMID: 23344959
  • It was shown that odorants directly activate CatSper without involving G protein-coupled receptors and cAMP. Membrane-permeable analogues of cyclic nucleotides activated CatSper directly via an extracellular site. PMID: 22354039
  • The decreased or abnormal expression of the CatSper1 protein may be a factor involved in the pathogenesis of idiopathic asthenozoospermia. PMID: 21404705
  • progesterone activates the sperm-specific, pH-sensitive CatSper Ca(2+) channel PMID: 21412338
  • human CatSper is synergistically activated by elevation of intracellular pH and extracellular progesterone PMID: 21412339
  • Studies indicate that CATSPER channel represents a novel human male fertility factor. PMID: 20648059
  • Potential role for CatSper in sperm motility and fertility in mouse and human. CatSper is therefore implicated as a potential target to explore the molecular mechanisms of male infertility. PMID: 14688170
  • CATSPER1 is meiotically and post-meiotically expressed in human testis tissue. PMID: 16625279
  • CatSper1 and CatSper2 can associate with and modulate the function of the Ca(v)3.3 channel, which might be important in the regulation of sperm function. PMID: 16740636
  • CatSper1 may be a potential target for immunocontraception, and the antibody may be a tool to study the function of ion channels in sperm. PMID: 18976756
  • sequence analysis of CATSPER1 in heritable forms of nonsyndromic male infertility revealed two separate insertion mutations (c.539-540insT and c.948-949insATGGC) that are predicted to lead to frameshifts and premature stop codons PMID: 19344877
  • FAQs

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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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