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1000 results found for “Calcyphosine”
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Name :
Calumenin Human, HisDescription:
Calumenin Human Recombinant, His Tag
CALU, Crocalbin, IEF SSP 9302, FLJ90608, Calumenin.
Product # :
PRO-696Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human Calumenin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 317 amino acids (20-315 a.a) and having a molecular mass of 37.2 kDa. Calumenin is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Calumenin protein contains 20mM Tris-HCl buffer pH-8 and 10% glycerol.
Purity
Greater than 90% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
Calumenin is a calcium-binding protein located in the endoplasmic reticulum (ER) and sarcoplasmic reticulum (SR) of mammalian tissues which plays a role in ER functions as protein folding and sorting. Calumenin belongs to a family of multiple EF-hand proteins (CERC) that include reticulocalbin, ERC-55, and Cab45 and the product of this gene. Calumenin binds 7 calcium ions having low affinity and takes part in such ER functions as protein folding and sorting.
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Synonyms
CALU, Crocalbin, IEF SSP 9302, FLJ90608, Calumenin.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MKPTEKKDRV HHEPQLSDKV HNDAQSFDYD HDAFLGAEEA KTFDQLTPEE SKERLGKIVS KIDGDKDGFV TVDELKDWIK FAQKRWIYED VERQWKGHDL NEDGLVSWEE YKNATYGYVL DDPDPDDGFN YKQMMVRDER RFKMADKDGD LIATKEEFTA FLHPEEYDYM KDIVVQETME DIDKNADGFI DLEEYIGDMY SHDGNTDEPE WVKTEREQFV EFRDKNRDGK MDKEETKDWI LPSDYDHAEA EARHLVYESD QNKDGKLTKE EIVDKYDLFV GSQATDFGEA LVRHDEF.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CAMK2N1 HumanDescription:
Calcium/Calmodulin Dependent Protein Kinase II Inhibitor 1 Human Recombinant
PRO1489; RP11-401M16.1, Calcium/calmodulin-dependent protein kinase II inhibitor 1, CaMKII inhibitory protein alpha, CaMKIIN-alpha, CAMK2N1.
Product # :
PRO-1873Price :
Quantity :
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Shipped with Ice Packs
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Description
CAMK2N1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (1-78 a.a) and having a molecular mass of 10.9kDa. CAMK2N1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CAMK2N1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Calcium/Calmodulin Dependent Protein Kinase II Inhibitor 1 (CAMK2N1), which interacts with CAMK2B, is a part of the CAMK2N family. CAMK2N1 is also interacts with CAMK2A in a way which requires CAMK2A activation by Ca2+. CAMK2N1 is potent and specific inhibitor of CaM-kinase II (CAMK2).
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Synonyms
PRO1489; RP11-401M16.1, Calcium/calmodulin-dependent protein kinase II inhibitor 1, CaMKII inhibitory protein alpha, CaMKIIN-alpha, CAMK2N1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSEVLPY GDEKLSPYGD GGDVGQIFSC RLQDTNNFFG AGQNKRPPKL GQIGRSKRVV IEDDRIDDVL KNMTDKAPPG V.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MIP 1a Mouse, HisDescription:
Macrophage Inflammatory Protein-1 Alpha Mouse Recombinant (CCL3), His Tag
Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA, TY-5, SIS-alpha, Heparin-binding chemotaxis protein, L2G25B.
Product # :
CHM-008Price :
Quantity :
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Shipped with Ice Packs
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Description
MIP-1a Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids (24-92 a.a.) and having a molecular mass of 10.4kDa.MIP-1a is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MIP-1a protein solution (0.5mg/ml) containing 20mM Sodium citrate buffer (pH 3.5) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophils and basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1 (IL-1), IL-6 and TNF-a from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.
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Synonyms
Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA, TY-5, SIS-alpha, Heparin-binding chemotaxis protein, L2G25B.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAPYGAD TPTACCFSYS RKIPRQFIVD YFETSSLCSQ PGVIFLTKRN RQICADSKET WVQEYITDLE LNA.
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Background
What is the molecular weight/Mw of MIP 1A MOUSE, HIS Protein?
MIP 1A MOUSE, HIS Protein has a total Mw of 10.4kDa.
What is the source or expression system of MIP 1A MOUSE, HIS Protein?
Escherichia Coli.
What is the Purity of MIP 1A MOUSE, HIS Protein?
MIP 1A MOUSE, HIS Protein is > 90% pure as determined by SDS-PAGE.
What is the Biological Activity of MIP 1A MOUSE, HIS Protein?
The biological functionality of MIP 1A MOUSE, HIS Protein will be determined in the future.
What is the amino acid sequence of MIP 1A MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSMAPYGAD TPTACCFSYS RKIPRQFIVD YFETSSLCSQ PGVIFLTKRN RQICADSKET WVQEYITDLE LNA..
What applications can MIP 1A MOUSE, HIS Protein be used in?
MIP 1A MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for MIP 1A MOUSE, HIS Protein?
The endotoxin level is minimal, MIP 1A MOUSE, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
S100G HumanDescription:
S100 Calcium Binding Protein G Human Recombinant
Protein S100-G, Calbindin-D9k, S100 calcium-binding protein G, Vitamin D-dependent calcium-binding protein intestinal, CABP, S100G, CABP9K, CALB3, S100D, CABP1, MGC138379.
Product # :
PRO-156Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Recombinant Human S100G produced in E.coli has a molecular mass of 10.04kDa containing 87 amino acid residues of the human S100G and fused to a 9 a.a. His tag at N-terminus.
Source
Escherichia Coli.
Formulation
S100G was filtered (0.4 µm) and lyophilized in 0.5 mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.
More Info
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Introduction
S100G (calbindin D9K) is a vitamin D-dependent calcium-binding protein. S100G, which is a cytosolic protein, is a member of a family of calcium-binding proteins that includes calmodulin, parvalbumin, troponin C, and S100 protein. In the intestine, S100G is vitamin D-dependent and its expression correlates with calcium transport activity. S100G may increase Ca2+ absorption by buffering Ca2+ in the cytoplasm and increase ATP-dependent Ca2+ transport in duodenal basolateral membrane vesicles.
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Synonyms
Protein S100-G, Calbindin-D9k, S100 calcium-binding protein G, Vitamin D-dependent calcium-binding protein intestinal, CABP, S100G, CABP9K, CALB3, S100D, CABP1, MGC138379.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS TKKSPEELKRS TKKSPEELKR IFEKYAAKEG DPDQLSKDEL KLLIQAEFPS LLKGPNTLDD LFQELDKNGD GEVSFEEFQV LVKKISQ.
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Applications
Western blotting.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Cyclophilin A MouseDescription:
Cyclophilin A Mouse Recombinant
Peptidyl-prolyl cis-trans isomerase A, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, SP18, Peptidyl-prolyl cis-trans isomerase A, N-terminally processed, Ppia, 2700098C05 Cphn, CyP-18, CypA.
Product # :
ENZ-857Price :
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Shipped with Ice Packs
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Description
Cyclophilin A Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids (1-164a.a.) and having a molecular mass of 20.4kDa.Cyclophilin A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
Cyclophilin A protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Cyclophilin-A is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. Cyclophilin-A can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported.
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Synonyms
Peptidyl-prolyl cis-trans isomerase A, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, SP18, Peptidyl-prolyl cis-trans isomerase A, N-terminally processed, Ppia, 2700098C05 Cphn, CyP-18, CypA.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMVNPTVF FDITADDEPL GRVSFELFAD KVPKTAENFR ALSTGEKGFG YKGSSFHRII PGFMCQGGDF TRHNGTGGRS IYGEKFEDEN FILKHTGPGI LSMANAGPNT NGSQFFICTA KTEWLDGKHV VFGKVKEGMN IVEAMERFGS RNGKTSKKIT ISDCGQL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Cyclophilin B MouseDescription:
Cyclophilin-B Mouse Recombinant
Peptidyl-prolyl cis-trans isomerase B, PPIase B, CYP-S1, Cyclophilin B, Rotamase B, S-cyclophilin, SCYLP.
Product # :
ENZ-1039Price :
Quantity :
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Shipped with Ice Packs
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Description
Cyclophilin B Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (34-216 a.a) and having a molecular mass of 22.7kDa.Cyclophilin B is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Cyclophilin B protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 1,000 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmole of suc-AAFP-PNA per minute at 37C in Tris–HCl pH 8.0 using chymotrypsin.
More Info
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Introduction
Cyclophilin B (also known as PPIB, peptidylpropyl isomerase B) is a cyclosporine-binding protein and is mainly located within the endoplasmic reticulum. It is associated with the secretory pathway and released in biological fluids. This protein can bind to cells derived from T- and B-lymphocytes, and may regulate cyclosporine A-mediated immunosuppression.
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Synonyms
Peptidyl-prolyl cis-trans isomerase B, PPIase B, CYP-S1, Cyclophilin B, Rotamase B, S-cyclophilin, SCYLP.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMNDKKKG PKVTVKVYFD LQIGDESVGR VVFGLFGKTV PKTVDNFVAL ATGEKGFGYK NSKFHRVIKD FMIQGGDFTR GDGTGGKSIY GERFPDENFK LKHYGPGWVS MANAGKDTNG SQFFITTVKT SWLDGKHVVF GKVLEGMDVV RKVESTKTDS
RDKPLKDVII VDSGKIEVEK PFAIAKE.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
S100A1 MouseDescription:
S100 Calcium Binding Protein A1 Mouse Recombinant
Protein S100-A1, S-100 protein alpha chain, S-100 protein subunit alpha, S100 calcium-binding protein A1, S100a1, S100, S100a, AI266795.
Product # :
PRO-237Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
S100A1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 114 amino acids (1-94 a.a) and having a molecular mass of 12.6kDa (molecular weight on SDS-PAGE will appear higher).S100A1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
S100A1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
S100A1 is a member of the S100 family of calcium binding proteins with EF-hand type Ca+2 binding motive. S100A1 (Calcium Binding Protein A1) is involved in the activation of sarcoplasmatic calcium release and the regulation of intermediate filament polymerization. S100A1 may function in stimulation of Ca2+-induced Ca2+ release, inhibition of microtubule assembly, and inhibition of protein kinase C-mediated phosphorylation. Reduced expression of S100A1 has been implicated in cardiomyopathies.
S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. -
Synonyms
Protein S100-A1, S-100 protein alpha chain, S-100 protein subunit alpha, S100 calcium-binding protein A1, S100a1, S100, S100a, AI266795.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSELESAME TLINVFHAHS GKEGDKYKLS KKELKDLLQT ELSGFLDVQK DADAVDKVMK ELDENGDGEV DFKEYVVLVA ALTVACNNFF WETS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
RCAN2 HumanDescription:
Regulator of Calcineurin 2 Human Recombinant
Regulator of calcineurin 2, DSCR1L1, MCIP2, Down syndrome critical region gene 1-like 1, ZAKI4, Myocyte-enriched calcineurin-interacting protein 2, Thyroid hormone-responsive protein ZAKI-4, CSP2, RCN2, thyroid hormone-responsive (skin fibroblasts).
Product # :
PRO-990Price :
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Shipping Method :
Shipped with Ice Packs
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Description
RCAN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids (1-197 a.a.) and having a molecular mass of 24.1kDa.RCAN2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
RCAN2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 200mM NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
RCAN2 is a member of the RCAN (Regulator of calcineurin) family that controls the activity of Calcineurin using a valine-rich region placed in their carboxyl tail. RCANs race against NFAT (nuclear factor of activated T-cells) to bind to the same docking site in calcineurin, and consequently inhibits or activates calcineurin activity. RCAN2 is a Ca(2+) dependent protein phosphatase which takes part in numerous neuornal functions.
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Synonyms
Regulator of calcineurin 2, DSCR1L1, MCIP2, Down syndrome critical region gene 1-like 1, ZAKI4, Myocyte-enriched calcineurin-interacting protein 2, Thyroid hormone-responsive protein ZAKI-4, CSP2, RCN2, thyroid hormone-responsive (skin fibroblasts).
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPAPSMDCDV STLVACVVDV EVFTNQEVKE KFEGLFRTYD DCVTFQLFKS FRRVRINFSN PKSAARARIE LHETQFRGKK LKLYFAQVQT PETDGDKLHL APPQPAKQFL ISPPSSPPVG WQPINDATPV LNYDLLYAVA KLGPGEKYEL HAGTESTPSV VVHVCDSDIE EEEDPKTSPK PKIIQTRRPG LPPSVSN
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CALM BovineDescription:
Calmodulin Bovine
Calmodulin, CaM, CALM.
Product # :
PRO-2800Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Source
Bovine brain tissue.
Formulation
CALM was lyophilized with 2mM EDTA.
Purity
Greater than 95.0%.
More Info
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Synonyms
Calmodulin, CaM, CALM.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CALM although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Calmodulin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CALM in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Applications
Biochemical and immunochemical investigations.
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Background
Role in Muscle Contraction and Relaxation:
In muscle cells, calmodulin plays a pivotal role in the regulation of contraction and relaxation. It interacts with myosin light-chain kinase during muscle contraction, initiating the process of cross-bridge cycling. Conversely, during muscle relaxation, calmodulin activates the enzyme myosin light-chain phosphatase, leading to the dephosphorylation of myosin and muscle relaxation. This delicate balance is crucial for proper muscle function.
Neuronal Signalling and Synaptic Plasticity:
In neurons, calmodulin is essential for neurotransmitter release and synaptic plasticity. It modulates the activity of proteins involved in vesicle fusion and neurotransmitter release. Additionally, calmodulin-dependent protein kinases (CaMKs) are critical for synaptic plasticity, learning, and memory. The intricate interplay between calmodulin and neuronal proteins underpins the fundamental processes of learning and cognition.
Implications in Disease and Therapeutics:
Dysregulation of calmodulin has been implicated in various diseases, including cardiac arrhythmias and neurodegenerative disorders. Mutations in calmodulin genes can lead to aberrant calcium signalling and cellular dysfunction. Consequently, understanding these molecular mechanisms offers potential therapeutic targets. Researchers are exploring calmodulin inhibitors and modulators for conditions like cardiac arrhythmias, aiming to restore normal cellular function.
Conclusion:
Calmodulin, with its remarkable structural versatility and central role in cellular signalling, epitomizes the complexity of biological regulation. Its influence spans from the fundamental processes of muscle contraction to the intricacies of neuronal signalling. Unravelling the mysteries of calmodulin not only deepens our understanding of basic biological phenomena but also holds the promise of innovative therapeutic interventions. This research illuminates calmodulin's significance, emphasizing its position as a master regulator in the orchestra of cellular life.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
S100A3 MouseDescription:
S100 Calcium Binding Protein A3 Mouse Recombinant
Protein S100-A3, Protein S-100E, S100 calcium-binding protein A3, S100a3, S100E.
Product # :
PRO-1166Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
S100A3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 125 amino acids (1-101 a.a) and having a molecular mass of 14.3kDa.S100A3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
S100A3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 2mM DTT and 150mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
S100A3 is part of S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm/nucleus of a broad range of cells, and takes part in the regulation of several cellular processes such as cell cycle progression and differentiation. S100A3 has the largest number of cysteines of all S100 proteins. S100A3 has high affinity for Zinc, and is widely expressed in human hair cuticle.
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Synonyms
Protein S100-A3, Protein S-100E, S100 calcium-binding protein A3, S100a3, S100E.
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Physical Appearance
S100A3 is supplied as a sterile filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMTRPLE QAVAAIVCTF QEYAGRCGDK YKICQSELKE LLQKELPTWT PSEFRECDYN KFMSVLDTNK DCEVDFGEYV RSLASLCLYC HEYFKECPPE PPCPQ.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CALML5 HumanDescription:
Calmodulin Like 5 Human Recombinant
CLSP, Calmodulin-like skin protein, CALML5, Calmodulin-like protein 5.
Product # :
PRO-2475Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CALML5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 2-146) containing 155 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 17.0kDa (calculated).
Source
Escherichia Coli.
Formulation
CALML5 filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20 mM Tris buffer, 50 mM NaCl and 5% w/v trehalosa, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Calmodulin Like 5, also known as CALML5 is a part of the calmodulin family of calcium binding proteins. CALML5 undergoes a conformational change as a result of binding calcium. CALML5 is taking part in terminal differentiation of keratinocytes and encodes a calcium binding protein expressed in the epidermis.
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Synonyms
CLSP, Calmodulin-like skin protein, CALML5, Calmodulin-like protein 5.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. CALML5 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS AGELTPEEEA QYKKAFSAVD TDGNGTINAQ ELGAALKATG KNLSEAQLRK LISEVDSDGD GEISFQEFLT AAKKARAGLE DLQVAFRAFD QDGDGHITVD ELRRAMAGLG QPLPQEELDA MIREADVDQD GRVNYEEFAR MLAQE.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CALML3 HumanDescription:
Calmodulin Like 3 Human Recombinant
Calmodulin-like protein 3, CaM-like protein, CLP, Calmodulin-related protein NB-1, CALML3.
Product # :
PRO-1323Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CALML3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 173 amino acids (1-149 a.a.) and having a molecular mass of 19kDa.CALML3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CALML3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Calmodulin Like 3 (CALML3) is a member of the calmodulin family and contains 4 EF-hand domains. The CALML3 protein may be similar to that of genuine calmodulin and may in fact compete with calmodulin by binding, with different affinities, to cellular substrates. CALML3 protein is expressed in normal mammary, prostate, cervical, and epidermal tissues.
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Synonyms
Calmodulin-like protein 3, CaM-like protein, CLP, Calmodulin-related protein NB-1, CALML3.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMADQLT EEQVTEFKEA FSLFDKDGDG CITTRELGTV MRSLGQNPTE AELRDMMSEI DRDGNGTVDF PEFLGMMARK MKDTDNEEEI REAFRVFDKD GNGFVSAAEL RHVMTRLGEK LSDEEVDEMI RAADTDGDGQ VNYEEFVRVL VSK.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CAMK2N1 MouseDescription:
Calcium/Calmodulin-Dependent Protein Kinase II Inhibitor 1 Mouse Recombinant
mCaMKIINalpha, calcium/calmodulin-dependent protein kinase II inhibitor alpha, Camk2n1.
Product # :
PKA-092Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CAMK2N1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (1-78 a.a) and having a molecular mass of 10.9kDa.CAMK2N1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CAMK2N1 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.5), 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Calcium/Calmodulin Dependent Protein Kinase II Inhibitor 1 (CAMK2N1), which interacts with CAMK2B, is a part of the CAMK2N family. CAMK2N1 is also interacts with CAMK2A in a way which requires CAMK2A activation by Ca2+. CAMK2N1 is potent and specific inhibitor of CaM-kinase II (CAMK2).
-
Synonyms
mCaMKIINalpha, calcium/calmodulin-dependent protein kinase II inhibitor alpha, Camk2n1.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSEVLPY GDEKLSPYGD GGDVGQIFSC RLQDTNNFFG AGQSKRPPKL GQIGRSKRVV IEDDRIDDVL KTMTDKAPPG V.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CALM HumanDescription:
Calmodulin Human
Calmodulin, CaM, CALM.
Product # :
PRO-2799Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Source
Human brain tissue.
Formulation
CALM was lyophilized with 2mM EDTA.
Purity
Greater than 95.0%.
More Info
-
Synonyms
Calmodulin, CaM, CALM.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized CALM although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Calmodulin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized CALM in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Applications
Blood samples from tissue donors were tested and found to be negative for syphilis, HBsAg, HIV-1 and HIV-2 antibodies and HCV.
-
Background
Calmodulin, a small, ubiquitous calcium-binding protein, stands as a linchpin in cellular signalling cascades. Its ability to modulate diverse cellular processes by transducing calcium signals has made it a focal point of scientific inquiry. With its role extending from muscle contraction to neurotransmitter release and gene expression, calmodulin orchestrates intricate physiological responses. This research delves into the multifaceted world of calmodulin, exploring its structural characteristics, calcium-binding properties, and its pivotal involvement in various biological pathways.
Structural Marvel of Calmodulin:
Calmodulin boasts a unique dumbbell-shaped structure, composed of four EF-hand motifs that enable it to bind calcium ions. When calcium binds to calmodulin, it undergoes a conformational change, allowing it to interact with a myriad of target proteins. This structural adaptability is fundamental to its ability to regulate a wide array of cellular activities.
Calcium Signalling and Transduction:
Intracellular calcium serves as a ubiquitous second messenger, and calmodulin is the key mediator of calcium signalling. When calcium levels rise, calmodulin binds calcium ions, triggering its activation. This activated form of calmodulin modulates the activity of various proteins, including enzymes, ion channels, and transcription factors. By doing so, calmodulin influences processes such as muscle contraction, neurotransmitter release, and cell proliferation.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PSPN MouseDescription:
Persephin Mouse Recombinant
Persephin, PSPN.
Product # :
CYT-802Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- biological activity
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Description
PSPN Mouse Recombinant produced in E.Coli is a disulfide-linked homodimer containing 2x96 amino acids and having a molecular mass of 20.7kDa. The PSPN is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2?m filtered concentrated solution in 30 %ACN, 0.1 %TFA, 150mM NaCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using human TT medullary thyroid cancer cells is less than 0.1ng/ml, corresponding to a specific activity of > 1.0 × 10,000,000 IU/mg.More Info
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Introduction
Persephin is a member of the GDNF ligand subfamily of the TGF-beta superfamily. PSPN encourages the existence and growth of key dopaminergic and motor neurons, as well as taking part in kidney development. Nonetheless, persephin does not support existence of peripheral neurons.
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Synonyms
Persephin, PSPN.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized PSPN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PSPN should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized PSPN in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
ALAGSCRLWS LTLPVAELGL GYASEEKVIF RYCAGSCPQE ARTQHSLVLA RLRGRGRAHG RPCCQPTSYA DVTFLDDQHH WQQLPQLSAA ACGCGG
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
S100A6 MouseDescription:
S100 Calcium Binding Protein A6 Mouse Recombinant
Protein S100-A6, S100 calcium-binding protein A6, Calcyclin, Prolactin receptor-associated protein, 5B10, S100a6, Cacy, 2A9, PRA.
Product # :
PRO-240Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
S100A6 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids (1-89 a.a) and having a molecular mass of 12.2kDa.S100A6 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
S100A6 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
S100A6 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21.
S100A6 may function in stimulation prolactin secretion, and exocytosis. Chromosomal rearrangements and altered expression of the S100A6 gene are implicated in melanoma. -
Synonyms
Protein S100-A6, S100 calcium-binding protein A6, Calcyclin, Prolactin receptor-associated protein, 5B10, S100a6, Cacy, 2A9, PRA.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MACPLDQAIG LLVAIFHKYS GKEGDKHTLS KKELKELIQK ELTIGSKLQD AEIARLMDDL DRNKDQEVNF QEYVAFLGAL ALIYNEALK.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
BCCIP HumanDescription:
BRCA2 And CDKN1A Interacting Protein Human Recombinant
BRCA2 and CDKN1A-interacting protein, P21- and CDK-associated protein 1, Protein TOK-1, BCCIP, TOK1, BRCA2 and CDKN1A-interacting protein.
Product # :
PRO-2014Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
BCCIP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 339 amino acids (1-314 a.a.) and having a molecular mass of 38.6kDa.BCCIP is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BCCIP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
BRCA2 And CDKN1A Interacting Protein (BCCIP) is a nuclear protein with multiple interacting domains which remained conserved throughout the evolution. BCCIP is an important cofactor for BRCA2 in tumor suppression, and a modulator of CDK2 kinase activity via p21. BCCIP takes also part in the regulation of BRCA2 and RAD51 nuclear focus formation, doublestrand break-induced homologous recombination, and cell cycle progression.
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Synonyms
BRCA2 and CDKN1A-interacting protein, P21- and CDK-associated protein 1, Protein TOK-1, BCCIP, TOK1, BRCA2 and CDKN1A-interacting protein.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEFMASRS KRRAVESGVP QPPDPPVQRD EEEEKEVENE DEDDDDSDKE KDEEDEVIDE EVNIEFEAYS LSDNDYDGIK KLLQQLFLKA PVNTAELTDL LIQQNHIGSV IKQTDVSEDS NDDMDEDEVF GFISLLNLTE RKGTQCVEQI QELVLRFCEK NCEKSMVEQL DKFLNDTTKP VGLLLSERFI NVPPQIALPM YQQLQKELAG AHRTNKPCGK CYFYLLISKT FVEAGKNNSK KKPSNKKKAA LMFANAEEEF FYEKAILKFN YSVQEESDTC LGGKWSFDDV PMTPLRTVML IPGDKMNEIM DKLKEYLSV.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CANX HumanDescription:
Calnexin Human Recombinant
Calnexin, Major histocompatibility complex class I antigen-binding protein p88, p90, IP90, CANX, CNX, FLJ26570.
Product # :
PRO-725Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CANX Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 462 amino acids (21-481 a.a.) and having a molecular mass of 52.5kDa.The CANX is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CANX protein solution contains 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Calnexin (CANX) belongs to the calnexin family of molecular chaperones. Calnexin is a calcium-binding, ER-associated protein that interacts briefly with newly synthesized N-linked glycoproteins, facilitating protein folding and assembly. Calnexin may also have a key role in the quality control of protein folding by retaining incorrectly folded protein subunits within the ER for degradation. Calnexin grants long-term protection of wild-type Shaker protein from ER-associated degradation. Polypeptide substrate recognition by Calnexin requires specific conformations of the Calnexin protein. Calnexin dwindles with aging and might contribute to a cytoprotection in an array of human age-related diseases.
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Synonyms
Calnexin, Major histocompatibility complex class I antigen-binding protein p88, p90, IP90, CANX, CNX, FLJ26570.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MHDGHDDDVI DIEDDLDDVI EEVEDSKPDT TAPPSSPKVT YKAPVPTGEV YFADSFDRGT LSGWILSKAK KDDTDDEIAK YDGKWEVEEM KESKLPGDKG LVLMSRAKHH AISAKLNKPF LFDTKPLIVQ YEVNFQNGIE CGGAYVKLLS KTPELNLDQF HDKTPYTIMF GPDKCGEDYK LHFIFRHKNP KTGIYEEKHA KRPDADLKTY FTDKKTHLYT LILNPDNSFE ILVDQSVVNS GNLLNDMTPP VNPSREIEDP EDRKPEDWDE RPKIPDPEAV KPDDWDEDAP AKIPDEEATK PEGWLDDEPE YVPDPDAEKP EDWDEDMDGE WEAPQIANPR CESAPGCGVW QRPVIDNPNY KGKWKPPMID NPSYQGIWKP RKIPNPDFFE DLEPFRMTPF SAIGLELWSM TSDIFFDNFI ICADRRIVDD WANDGWGLKK AADGAAEPGV VGQMIEAAEE RP.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CAPZA2 HumanDescription:
Capping Protein (Actin Filament) Muscle Z-Line Alpha 2 Human Recombinant
Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2, F-Actin Capping Protein Alpha-2 Subunit, CapZ Alpha-2, CAPPA, CAPZ2, F-Actin-Capping Protein Subunit Alpha-2.
Product # :
PRO-1721Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CAPZA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 309 amino acids (1-286 a.a) and having a molecular mass of 35.3kDa.CAPZA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CAPZA2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, and 0.4M UREA.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2 also known as CAPZA2 belongs the F-actin capping protein alpha subunit family. It is the alpha subunit of the barbed-end actin binding protein Cap Z. By capping the barbed end of actin filaments, Cap Z regulates the growth of the actin filaments at the barbed end. Among the diseases associated with CAPZA2 are endocarditis, and cervicitis.
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Synonyms
Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2, F-Actin Capping Protein Alpha-2 Subunit, CapZ Alpha-2, CAPPA, CAPZ2, F-Actin-Capping Protein Subunit Alpha-2.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMADLEEQ LSDEEKVRIA AKFIIHAPPG EFNEVFNDVR LLLNNDNLLR EGAAHAFAQY NLDQFTPVKI EGYEDQVLIT EHGDLGNGKF LDPKNRICFK FDHLRKEATD PRPCEVENAV ESWRTSVETA LRAYVKEHYP NGVCTVYGKK IDGQQTIIAC IESHQFQAKN FWNGRWRSEW KFTITPSTTQ VVGILKIQVH YYEDGNVQLV SHKDIQDSLT VSNEVQTAKE FIKIVEAAEN EYQTAISENY QTMSDTTFKA LRRQLPVTRT KIDWNKILSY KIGKEMQNA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CCL28 MouseDescription:
Mucosae-Associated Epithelial Chemokine Mouse Recombinant (CCL28)
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
Product # :
CHM-369Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CCL28 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids and having a molecular mass of 12.6 kDa. The CCL28 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM Phosphate buffer pH-7.4 and 150mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract mouse lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.More Info
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Introduction
CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues. -
Synonyms
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CCL28 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL28 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CCL28 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SEAILPMASS CCTEVSHHVS GRLLERVSSC SIQRADGDCD LAAVILHVKR RRICISPHNR TLKQWMRASE VKKNGRENVC SGKKQPSRKD RKGHTTRKHR TRGTHRHEAS R.
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Background
What is the molecular weight/Mw of CCL28 MOUSE Protein?
CCL28 MOUSE Protein has a total Mw of 12.6kDa.
What is the source or expression system of CCL28 MOUSE Protein?
Escherichia Coli.
What is the Purity of CCL28 MOUSE Protein?
CCL28 MOUSE Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL28 MOUSE Protein?
Determined by its ability to chemoattract mouse lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of CCL28 MOUSE Protein?
SEAILPMASS CCTEVSHHVS GRLLERVSSC SIQRADGDCD LAAVILHVKR RRICISPHNR TLKQWMRASE VKKNGRENVC SGKKQPSRKD RKGHTTRKHR TRGTHRHEAS R.
What applications can CCL28 MOUSE Protein be used in?
CCL28 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL28 MOUSE Protein?
The endotoxin level is minimal, CCL28 MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IFNG MouseDescription:
IFN-Gamma Mouse Recombinant
Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.
Product # :
CYT-358Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IFN-gamma Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids and having a molecular mass of 15.6kDa.The IFN-gamma is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4 and 5% trehalose.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined in a viral resistance assay is < 0.1 ng/ml, corresponding to a specific activity of 10,000,000 IU/mg
More Info
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Introduction
IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I IFNs. -
Synonyms
Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized IFN-gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-gamma should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized IFN-gamma in sterile distilled water or 20mM AcOH at concentrations ranging between 0.1mg-0.5mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MHGTVIESLE SLNNYFNSSG IDVEEKSLFL DIWRNWQKDG DMKILQSQII SFYLRLFEVL KDNQAISNNI SVIESHLITT FFSNSKAKKD AFMSIAKFEV NNPQVQRQAF NELIRVVHQL LPESSLRKRK RSRC.
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Background
What is the molecular weight/Mw of IFNG MOUSE Protein?
IFNG MOUSE Protein has a total Mw of 15.6kDa.
What is the source or expression system of IFNG MOUSE Protein?
Escherichia Coli.
What is the Purity of IFNG MOUSE Protein?
IFNG MOUSE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNG MOUSE Protein?
The specific activity as determined in a viral resistance assay is < 0.1 ng/ml, corresponding to a specific activity of 10,000,000 IU/mg
What is the amino acid sequence of IFNG MOUSE Protein?
MHGTVIESLE SLNNYFNSSG IDVEEKSLFL DIWRNWQKDG DMKILQSQII SFYLRLFEVL KDNQAISNNI SVIESHLITT FFSNSKAKKD AFMSIAKFEV NNPQVQRQAF NELIRVVHQL LPESSLRKRK RSRC.
What applications can IFNG MOUSE Protein be used in?
IFNG MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNG MOUSE Protein?
The endotoxin level is minimal, IFNG MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TNF a MouseDescription:
Tumor Necrosis Factor-Alpha Mouse Recombinant
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Product # :
CYT-252Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Tumor Necrosis Factor-a Mouse Recombinant produced in E. coli is a single, non glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17301.32 Dalton. The TNF-alpha is purified by standard chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(c) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.1ng/ml, corresponding to a Specific Activity of 10,000,000 Units/mg.More Info
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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer. -
Synonyms
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Tumor Necrosis Factor-alpha in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MLRSSSQNSS DKPVAHVVAN HQVEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLVY SQVLFKGQGC PDYVLLTHTV SRFAISYQEK VNLLSAVKSP CPKDTPEGAE LKPWYEPIYL GGVFQLEKGD QLSAEVNLPK YLDFAESGQV YFGVIAL
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Background
Tumor Necrosis Factor-alpha (TNF-α) is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. It is primarily produced by activated macrophages, but can also be secreted by other immune cells, such as T cells, natural killer cells, and mast cells. TNF-α is involved in a wide range of physiological and pathological processes, including the defense against infections, the development of autoimmune diseases, and the progression of cancer.
TNF-α exerts its effects by binding to two distinct cell surface receptors, TNF receptor 1 (TNFR1) and TNF receptor 2 (TNFR2). Upon binding to its receptors, TNF-α activates multiple signaling pathways, including the nuclear factor-kappa B (NF-κB) pathway, the mitogen-activated protein kinase (MAPK) pathway, and the apoptotic pathway. These signaling pathways regulate various cellular processes, such as inflammation, cell proliferation, differentiation, and apoptosis.
In the context of infections, TNF-α plays a crucial role in the body's defense against pathogens. It promotes the recruitment and activation of immune cells, enhances the production of other pro-inflammatory cytokines, and stimulates the expression of adhesion molecules on endothelial cells, facilitating the migration of immune cells to the site of infection. TNF-α also helps to induce fever, which is an important component of the body's immune response to infections.
However, excessive or prolonged production of TNF-α can contribute to the development of chronic inflammatory diseases, such as rheumatoid arthritis, inflammatory bowel disease, and psoriasis. In these conditions, elevated levels of TNF-α promote the infiltration of immune cells into the affected tissues, leading to tissue damage and the perpetuation of inflammation. The central role of TNF-α in the pathogenesis of these diseases has led to the development of anti-TNF-α therapies, which have revolutionized the treatment of chronic inflammatory diseases. These therapies include monoclonal antibodies, such as infliximab and adalimumab, and soluble TNF receptor fusion proteins, such as etanercept. Anti-TNF-α therapies have been shown to be effective in reducing inflammation, improving symptoms, and slowing disease progression in patients with chronic inflammatory diseases.
In the context of cancer, TNF-α has complex and context-dependent effects on tumor development and progression. On one hand, TNF-α can promote anti-tumor immunity by activating immune cells and stimulating the production of other pro-inflammatory cytokines. On the other hand, chronic inflammation driven by TNF-α can promote tumor growth, angiogenesis, and metastasis. Therefore, the role of TNF-α in cancer is still an area of active research, and the development of TNF-α-targeted therapies for cancer remains a challenge.
In conclusion, TNF-α is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. Its involvement in various physiological and pathological processes has made it an important target for the development of therapies for chronic inflammatory diseases and cancer. Anti-TNF-α therapies have revolutionized the treatment of chronic inflammatory diseases, but the complex role of TNF-α in cancer remains an area of ongoing research. Understanding the precise mechanisms by which TNF-α contributes to disease pathogenesis will be crucial for the development of more effective and targeted therapies.
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Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.24 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of TNF-a as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CALM2 Human 135 a.aDescription:
Calmodulin-2 135 a.a. Human Recombinant
CALM2, CAM2, CAMB, CAMII, PHKD2, calmodulin 2.
Product # :
PRO-370Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CALM2 Human Recombinant full length protein expressed in E.coli, containing 135 amino acids and having a Molecular Weight of approximately 16 kDa.
Source
Escherichia Coli.
Formulation
CALM2 at 1mg/ml in 20mM HEPES-KOH, pH7, 50mM NaCl, 1mM EDTA and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Calmodulin (CaM) is an intracellular receptor protein for Ca2+-ions. It activates the myosin light chain kinase which is the catalyst of myosin phosphorylation. CaM participates in the activation of enzymes such as cyclic nucleotide- dependent phosphodiesterase, calcineurin, ATPase, Myosin Light Chain Kinases, and CAM kinase.
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Synonyms
CALM2, CAM2, CAMB, CAMII, PHKD2, calmodulin 2.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE EVDEMIREAD IDGDGQ.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CLCF1 HumanDescription:
Neurotrophin-1 Human Recombinant
Cardiotrophin-Like Cytokine Factor 1, Novel Neurotrophin-1 , BSF3, CLC, CRLF1 Associated Cytokine-Like Factor 1, B-Cell Stimulating Factor 3, B-Cell-Stimulating Factor 3, BSF-3, NNT-1, NNT1, Neurotrophin-1/B-Cell Stimulating Factor-3, Cold-Induced Sweating Syndrome 2, B-Cell Stimulatory Factor 3, CISS2, NR6, CLCF1.
Product # :
CYT-869Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Neurotrophin-1 Human Recombinant (28-225) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 199 amino acids and having a molecular mass of 22kDa.The NNT-1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NNT-1 protein was lyophilized from a 0.2µm filtered solution in Acetonitrile and TFA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured in a cell proliferation assay using human TF?1 cells transfected with human CNTF R?, is less than 15ng/ml.More Info
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Introduction
Cardiotrophin-like cytokine (CLC/ NNT-1) belongs to the IL-6 family of cytokines. All family members share the receptor subunit gp130, which belongs to the type I cytokine receptor superfamily. NNT1 is a trophic factor for motor neurons, a stimulator of ACTH release from corticotrophs, and an inducer of IgE synthesis and B cell proliferation. Cells expressing NNT-1 include embryonic muscle, lung epithelium, and mesenchyme. NNT1 binds to and activates the ILST/gp130 receptor.
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Synonyms
Cardiotrophin-Like Cytokine Factor 1, Novel Neurotrophin-1 , BSF3, CLC, CRLF1 Associated Cytokine-Like Factor 1, B-Cell Stimulating Factor 3, B-Cell-Stimulating Factor 3, BSF-3, NNT-1, NNT1, Neurotrophin-1/B-Cell Stimulating Factor-3, Cold-Induced Sweating Syndrome 2, B-Cell Stimulatory Factor 3, CISS2, NR6, CLCF1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Neurotrophin-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NNT1 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized NNT1 in sterile 18M-cm H2O not less than 0.5mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MLNRTGDPGP GPSIQKTYDL TRYLEHQLRS LAGTYLNYLG PPFNEPDFNP PRLGAETLPR ATVDLEVWRS LNDKLRLTQN YEAYSHLLCY LRGLNRQAAT AELRRSLAHF CTSLQGLLGS IAGVMAALGY PLPQPLPGTE PTWTPGPAHS DFLQKMDDFW LLKELQTWLW RSAKDFNRLK KKMQPPAAAV TLHLGAHGF.
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Background
What is the molecular weight/Mw of CLCF Protein?
CLCF Protein has a total Mw of 22kDa.
What is the source or expression system of CLCF Protein?
Escherichia Coli.
What is the Purity of CLCF Protein?
CLCF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CLCF Protein?
The ED50, as measured in a cell proliferation assay using human TF?1 cells transfected with human CNTF R?, is less than 15ng/ml.
What is the amino acid sequence of CLCF Protein?
MLNRTGDPGP GPSIQKTYDL TRYLEHQLRS LAGTYLNYLG PPFNEPDFNP PRLGAETLPR ATVDLEVWRS LNDKLRLTQN YEAYSHLLCY LRGLNRQAAT AELRRSLAHF CTSLQGLLGS IAGVMAALGY PLPQPLPGTE PTWTPGPAHS DFLQKMDDFW LLKELQTWLW RSAKDFNRLK KKMQPPAAAV TLHLGAHGF.
What applications can CLCF Protein be used in?
CLCF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CLCF Protein?
The endotoxin level is minimal, CLCF Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.