Product Description
Monoclonal Antibody for studying S100A1. Validated for IHC Leica Bond,Immunohistochemistry (Paraffin). Available in 2 sizes. Highly specific and rigorously validated in-house, S100A1 (4C4.9) Mouse Monoclonal Antibody (CST #64095) is ready to ship.
Product Usage Information
IHC Leica Bond: 1:800 - 1:3200
Immunohistochemistry (Paraffin): 1:400 - 1:1600
Storage
Supplied in a PBS-based buffer with ~1% BSA and less than 0.1% sodium azide. Stable for 6 months when stored at 4°C. Do not aliquot the antibody. Note: This product is only available in the format listed above. We are unable to provide this in a carrier free, custom formulation.
Protocol
Available protocols: IHC Leica Bond, Immunohistochemistry (Paraffin)
Specificity / Sensitivity
S100A1 (4C4.9) Mouse Monoclonal Antibody recognizes endogenous levels of S100A1 protein.
Species Reactivity: Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a purified bovine brain S100A1 protein.
Background
Despite their relatively small size (8-12 kDa) and uncomplicated architecture, S100 proteins regulate a variety of cellular processes, such as cell growth and motility, cell cycle progression, transcription, and differentiation. To date, 25 members have been identified, including S100A1-S100A18, trichohyalin, filaggrin, repetin, S100P, and S100Z, making it the largest group in the EF-hand, calcium-binding protein family. Interestingly, 14 S100 genes are clustered on human chromosome 1q21, a region of genomic instability. Research studies have demonstrated that significant correlation exists between aberrant S100 protein expression and cancer progression. S100 proteins primarily mediate immune responses in various tissue types but are also involved in neuronal development (1-4). Each S100 monomer bears two EF-hand motifs and can bind up to two molecules of calcium (or other divalent cations in some instances). Structural evidence shows that S100 proteins form antiparallel homo- or heterodimers that coordinate binding partner proximity in a calcium-dependent (and sometimes calcium-independent) manner. Although structurally and functionally similar, individual members show restricted tissue distribution, are localized in specific cellular compartments, and display unique protein binding partners, which suggests that each plays a specific role in various signaling pathways. In addition to an intracellular role, some S100 proteins have been shown to act as receptors for extracellular ligands or are secreted and exhibit cytokine-like activities (1-4). S100A1 is abundantly expressed in cardiac and skeletal muscle where it plays a major role in regulating calcium-dependent contractility (5,6). S100A1 and calmodulin bind and differentially regulate ryanodine receptors (RyRs), thereby modulating skeletal and cardiac muscle function (7). In addition to RyRs (RyR1 and RyR2), S100A1 has also been shown to interact with other components of the calcium-dependent cardiac signaling cascade, including SERCA2a and phospholamban (8). Studies in animal models strongly suggest that S100A1 plays a significant role in the development of heart failure (1). In non-cardiac tissues, S100A1 has been shown to regulate cytoskeletal signaling, neurotransmitter release, enzymatic activity, transcription factors, and other calcium-binding proteins via direct interaction or via regulation of scaffolding and signaling components in each pathway (4).
Alternate Names
Protein S100-A1; S-100 protein alpha chain; S-100 protein subunit alpha; S100; S100 alpha; S100 calcium binding protein A1; S100 calcium-binding protein A1; S100 protein; S100 protein, alpha polypeptide; S100-alpha; S100A; S100A1; S10A1
Specification
REACTIVITY: H
SENSITIVITY: Endogenous
Source/Isotype: Mouse IgG2a kappa
Order Guidelines
1. Price & Stock Available on Request. Click to send email to: service@iright.com
2. Please DO NOT make payment before confirmation.
3. Minimum order value of $1,000 USD required.
Collaboration
Tony Tang
Email: Tony.Tang@iright.com
Mobile/WhatsApp/Wechat: +86-17717886924