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1000 results found for “f-box protein”
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Name :
TAGLN3 HumanDescription:
Transgelin-3 Human Recombinant
Transgelin 3, NP22, NP25, Neuronal protein 22, Neuronal protein NP25.
Product # :
PRO-946Price :
Quantity :
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Shipped with Ice Packs
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Description
TAGLN3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 219 amino acids (1-199) and having a molecular mass of 24.6 kDa.The TAGLN3 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TAGLN3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
TAGLN3 holds a putative Actin-binding domain, two potential phosphorylation sites, two EF-hand motifs and a calponin-homology (CH) domain. TAGLN3 is homologic to transgelin and calponin, two cytoskeleton-interacting proteins. TAGLN3 is a member of the calponin family, and is co-localized with Actin and tubulin, which indicates that TAGLN3 has a part in neuronal plasticity or as a signaling protein. As a result of a wide-ranging expression pattern, TAGLN3 is able to take different roles in the developing and adult brain.
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Synonyms
Transgelin 3, NP22, NP25, Neuronal protein 22, Neuronal protein NP25.
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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 MANRGPSYGL SREVQEKIEQ KYDADLENKL VDWIILQCAE DIEHPPPGRA HFQKWLMDGT VLCKLINSLY PPGQEPIPKI SESKMAFKQM EQISQFLKAA ETYGVRTTDI FQTVDLWEGK DMAAVQRTLM ALGSVAVTKD DGCYRGEPSW FHRKAQQNRR GFSEEQLRQG QNVIGLQMGS NKGASQAGMT GYGMPRQIM
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 :
SCG5 HumanDescription:
Secretogranin-V Human Recombinant
7B2, SgV, P7B2, SGNE1, Secretogranin-5, Secretory granule endocrine protein I.
Product # :
PRO-467Price :
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Shipped with Ice Packs
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Description
SCG5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 195 amino acids (27-212 a.a.) and having a molecular mass of 22 kDa. SCG5 is fused to a 8 amino acid His tag at C-terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
SCG5 solution (0.5mg/ml) containing 20mM Tris-HCl pH-8, 0.1mM PMSF, 1mM DTT, 0.1M NaCl and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
SCG5 also called 7B2 protein is localized in neuroendocrine tissues. SCG5 functions as a chaperone protein for the proprotein convertase PC2 and is essential for the production of an active PC2 enzyme.
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Synonyms
7B2, SgV, P7B2, SGNE1, Secretogranin-5, Secretory granule endocrine protein I.
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Physical Appearance
Sterile Filtered colorless liquid formulation.
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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.Please avoid freeze thaw cycles.
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Amino Acid Sequence
MYSPRTPDRV SEADIQRLLH GVMEQLGIAR PRVEYPAHQA MNLVGPQSIE GGAHEGLQHL GPFGNIPNIV AELTGDNIPK DFSEDQGYPD
PPNPCPVGKT ADDGCLENTP DTAEFSREFQ LHQHLSDPEH DYPGLGKWNK KLLYEKMKGG ERRKRRSVNP YLQGQRLDNV VAKKSVPHFS
DEDKDPELEH HHHHH.
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 :
FABP4 HumanDescription:
Fatty Acid Binding Protein 4 Human
Fatty acid-binding protein adipocyte, AFABP, Fatty acid-binding protein 4, Adipocyte lipid-binding protein, ALBP, A-FABP, FABP4.
Product # :
PRO-1568Price :
Quantity :
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Shipped at Room temp
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Description
The Human FABP4 produced from Human Adipose Tissue has a molecular mass of 14.587kDa (calculated without glycosylation) containing 131 amino acid residues.
Source
Human Adipose Tissue.
Formulation
FABP4 protein filtered (0.4µm) and lyophilized in 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 6.5.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Adipocyte fatty acid binding protein FABP4 is a 15 kDa member of the intracellular fatty acid binding protein (FABP) family, which is known for the ability to bind fatty acids and related compounds (bile acids or retinoids) in an internal cavity. FABP4 is expressed in a differentiation-dependent fashion in adipocytes and is a critical gene in the regulation of the biological function of these cells.
In mice, targeted mutations in FABP4 provide significant protection from IR in the context of both dietary and genetic obesity. Adipocytes obtained from FABP4-deficient mice also have reduced efficiency of ipolysis in vitro and in vivo, and these mice exhibited moderately improved systemic dyslipidemia. Recent studies also demonstrated FABP4 expression in macrophages upon differentiation and activation. In these cells, FABP4 modulates inflammatory responses and cholesterol ester accumulation, and total or macrophage-specific FABP4 deficiency confers dramatic protection against atherosclerosis in the apoE-/- mice. These results indicate a central role for FABP4 in the development of major components of the metabolic syndrome through its distinct actions in adipocytes and macrophages. -
Synonyms
Fatty acid-binding protein adipocyte, AFABP, Fatty acid-binding protein 4, Adipocyte lipid-binding protein, ALBP, A-FABP, FABP4.
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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 0.5 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
CDAFVGTWKL VSSENFDDYM KEVGVGFATR KVAGMAKPNM IISVNGDVIT IKSESTFKNT EISFILGQEF DEVTADDRKV KSTITLDGGV LVHVQKWDGK STTIKRKRED DKLVVECVMK GVTSTRVYER A.
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 :
IFN a 2b Human, YeastDescription:
Interferon-Alpha 2b Human Recombinant, Yeast
Interferon alpha 2b, IFNA, INFA2, IFN-? 2b, MGC125764, MGC125765.
Product # :
CYT-460Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interferon-alpha 2b Human Recombinant produced in yeast is a single, glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of approximately 19.3 kDa.The IFN-a 2b is purified by proprietary chromatographic techniques.
Source
Saccharomyces cerevisiae.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH-7.4 and 0.02% Tween-20.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined by an anti-viral assay was found to be no less than 1.6 x108IU/mg.
More Info
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Introduction
IFN-alpha is produced by macrophages and has antiviral activities. Interferon stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.
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Synonyms
Interferon alpha 2b, IFNA, INFA2, IFN-? 2b, MGC125764, MGC125765.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized glycosilated IFN-a 2b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-alpha 2b 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 glycosilated IFN alpha 2b 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
CDLPQTHSLG SRRTLMLLAQ MRRISLFSCL KDRHDFGFPQ EEFGNQFQKA ETIPVLHEMI QQIFNLFSTK DSSAAWDETL LDKFYTELYQ QLNDLEACVI QGVGVTETPL MKEDSILAVR KYFQRITLYL KEKKYSPCAW EVVRAEIMRS FSLSTNLQES LRSKE.
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Background
What is the molecular weight/Mw of IFN A 2B HUMAN, YEAST Protein?
IFN A 2B HUMAN, YEAST Protein has a total Mw of 19.3kDa.
What is the source or expression system of IFN A 2B HUMAN, YEAST Protein?
Saccharomyces cerevisiae.
What is the Purity of IFN A 2B HUMAN, YEAST Protein?
IFN A 2B HUMAN, YEAST Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of IFN A 2B HUMAN, YEAST Protein?
The specific activity as determined by an anti-viral assay was found to be no less than 1.6 x108IU/mg.
What is the amino acid sequence of IFN A 2B HUMAN, YEAST Protein?
CDLPQTHSLG SRRTLMLLAQ MRRISLFSCL KDRHDFGFPQ EEFGNQFQKA ETIPVLHEMI QQIFNLFSTK DSSAAWDETL LDKFYTELYQ QLNDLEACVI QGVGVTETPL MKEDSILAVR KYFQRITLYL KEKKYSPCAW EVVRAEIMRS FSLSTNLQES LRSKE.
What applications can IFN A 2B HUMAN, YEAST Protein be used in?
IFN A 2B HUMAN, YEAST Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFN A 2B HUMAN, YEAST Protein?
The endotoxin level is minimal, IFN A 2B HUMAN, YEAST 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 :
Myo Human w/o HDescription:
Myoglobin (Heme free) Human Recombinant
Myoglobin, MB, PVALB, MGC13548.
Product # :
PRO-374Price :
Quantity :
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Shipped with Ice Packs
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Description
Myoglobin heme free Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 11.67 kDa. The Myoglobin heme free contains N-terminal T7 tag and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The sterile solution contains phosphate-buffered saline (pH 8.0) and 50mM phosphate-borate.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Myoglobin is a member of the globin superfamily and can be found in skeletal and cardiac muscles. It is a haemoprotein that contributs to intracellular oxygen storage and transcellular facilitated diffusion of oxygen. Myoglobin has a single-chain globular structure of 153 amino acids, containing a heme prosthetic group (iron-containing porphyrin) in the core around which the remaining apoprotein folds. Myoglobin has 8 alpha helices and a hydrophobic core. Myoglobin’s molecular weight is 16.7 kDa, and it is the primary oxygen-carrying pigment of muscle tissues. The binding of oxygen in myoglobin is different from the cooperative oxygen binding in hemoglobin, since positive collaboration is a property of multimeric/oligomeric proteins only. Instead, the binding of oxygen by myoglobin is uninfluenced by the oxygen pressure in the surrounding tissue. Myoglobin is frequently referred to as having an "instant binding tenacity" to oxygen given its hyperbolic oxygen dissociation curve. Different organisms are able to hold their breaths longer due to high concentrations of myoglobin in their muscle cells. Myoglobin is responsible for the pigments that make meat red. The color of the meat is partly determined by the charge of the iron atom in myoglobin and the oxygen attached to it. Myoglobin is found in Type I muscle, Type II A and Type II B, but it is mostly deemed that myoglobin is not found in smooth muscle. Myoglobin is discharged from damaged muscle tissue (rhabdomyolysis), which contains very high concentrations of myoglobin. Even though the released myoglobin is filtered by the kidneys, it is toxic to the renal tubular epithelium and thus may cause acute renal failure.
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Synonyms
Myoglobin, MB, PVALB, MGC13548.
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Physical Appearance
Sterile Filtered solution.
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Stability
Myoglobin heme free although stable at 15°C for 2 weeks, should be stored at 4°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please do not freeze.
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 :
FABP3 Human, HisDescription:
Fatty Acid Binding Protein 3 Human Recombinant, His Tag
Fatty acid-binding protein heart, H-FABP, Heart-type fatty acid-binding protein, Muscle fatty acid-binding protein, M-FABP, Mammary-derived growth inhibitor, MDGI, FABP3, FABP11, O-FABP.
Product # :
PRO-668Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FABP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 133 amino acids and having a molecular mass of 19.1 kDa. FABP3 is fused to a 37 amino acid His tag at N-terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
FABP3 His-Tag is supplied in 20mM Tris-HCl pH 8.0 and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Recombinant Fatty Acid Binding Protein is a newly introduced plasma marker of acute myocardial infarction (AMI). The plasma kinetics of FABP (15kD) closely resemble those of myoglobin in that elevated plasma concentrations are found within 2 hours after AMI and return to normal generally within 18 to 24 hours. But the concentration of FABP in the skeletal muscle is 20 times lower than in cardiac tissue (for myoglobin the same content for cardiac and skeletal tissue), that makes FABP to be more cardiac specific than myoglobin. This makes FABP a useful biochemical marker for the early assessment or exclusion of AMI. FABP also appears to be a useful plasma marker for the estimation of myocardial infarct size.
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Synonyms
Fatty acid-binding protein heart, H-FABP, Heart-type fatty acid-binding protein, Muscle fatty acid-binding protein, M-FABP, Mammary-derived growth inhibitor, MDGI, FABP3, FABP11, O-FABP.
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Physical Appearance
Sterile Filtered colorless liquid formulation.
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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.Please avoid freeze thaw cycles.
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 :
CHP HumanDescription:
Calcium Binding Protein P22 Human Recombinant
CHP, CHP Human, Calcium-binding protein p22, Calcium-binding protein CHP, Calcineurin homologous protein, Calcineurin B homolog, SLC9A1BP.
Product # :
PRO-847Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CHP Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (1-195 a.a.) and having a molecular mass of 24.7 kDa. The CHP is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CHP Human solution containing 20mM Tris-HCl pH-7.5 & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Calcium-binding protein P22 is a phosphoprotein that binds to the sodium-hydrogen exchangers (NHEs). CHP is an essential cofactor which maintains the physiological activity of NHE family members. CHP has protein sequence resemblance to calcineurin B and it is also identified to be an endogenous inhibitor of calcineurin activity.CHP is necessary for constitutive membrane traffic. CHP Inhibits GTPase-stimulated Na(+)/H(+) exchange. CHP inhibits calcineurin phosphatase activity. Required for activity of SLC9A1/NHE1.
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Synonyms
CHP, CHP Human, Calcium-binding protein p22, Calcium-binding protein CHP, Calcineurin homologous protein, Calcineurin B homolog, SLC9A1BP.
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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 MMGSRASTLL RDEELEEIKK ETGFSHSQIT RLYSRFTSLD KGENGTLSRE DFQRIPELAI NPLGDRIINA FFPEGEDQVN FRGFMRTLAH FRPIEDNEKS KDVNGPEPLN SRSNKLHFAF RLYDLDKDEK ISRDELLQVL RMMVGVNISD EQLGSIADRT IQEADQDGDS AISFTEFVKV LEKVDVEQKM SIRFLH.
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 :
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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 :
UBL3 HumanDescription:
Ubiquitin-Like 3 Human Recombinant
Ubiquitin-like 3, FLJ32018, HCG-1, Membrane-anchored ubiquitin-fold protein, MUB, PNSC1, HsMUB, DKFZP434K151.
Product # :
PRO-230Price :
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Shipping Method :
Shipped with Ice Packs
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Description
UBL3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 134 amino acids (1-114a.a) and having a molecular mass of 15.0kDa.UBL3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UBL3 protein solution (1mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
UBL3 - a member of the ubiquitin-like family is found in the membrane. UBL3 holds two N-glycosylation sites, a C-terminal prenylation site and a protein kinase C phosphorylation site. Even though Ubiquitin-like proteins are not directly involved in protein degradation, it seems they have several mechanistic similarities to the ubiquitin pathway.
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Synonyms
Ubiquitin-like 3, FLJ32018, HCG-1, Membrane-anchored ubiquitin-fold protein, MUB, PNSC1, HsMUB, DKFZP434K151.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
UBL3 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSSNVPADMI NLRLILVSGK TKEFLFSPND SASDIAKHVY DNWPMDWEEE QVSSPNILRL IYQGRFLHGN VTLGALKLPF GKTTVMHLVA RETLPEPNSQ GQRNREKTGE SNCC
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 :
PFDN1 HumanDescription:
Prefoldin Subunit 1 Human Recombinant
Prefoldin subunit 1, PFDN1, PFD1, PDF.
Product # :
PRO-277Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PFDN1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 130 amino acids (14-122 a.a.) and having a molecular mass of 15kDa. The PFDN1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PFDN1 solution (0.5 mg/ml) contains 20mM Tris-HCl Buffer (pH 8.0) and 20% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
PFDN1 is one of 6 subunits of prefoldin, which is a heterohexameric chaperone protein that assists in the proper folding of other proteins. The PFDN1 protein delivers nonnative target proteins, primarily actins and tubulins, to the eukaryotic cytosolic chaperonin for facilitated folding. Defects in PFDN1 presented phenotypes typical of defects in cytoskeletal function, including manifestations of ciliary dyskinesia, neuronal loss, and defects in B and T cell development and function.
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Synonyms
Prefoldin subunit 1, PFDN1, PFD1, PDF.
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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 MTELQAKVID TQQKVKLADI QIEQLNRTKK HAHLTDTEIM TLVDETNMYE GVGRMFILQS KEAIHSQLLE KQKIAEEKIK ELEQKKSYLE RSVKEAEDNI REMLMARRAQ.
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 :
CECR1 HumanDescription:
Cat Eye Syndrome Chromosome Region Candidate 1 Human Recombinant
Cat Eye Syndrome Chromosome Region, Candidate 1, Cat Eye Syndrome Critical Region Protein 1, IDGFL, ADA2, ADGF, Adenosine Deaminase 2, EC 3.5.4.4, SNEDS, PAN, CECR1.
Product # :
PRO-2323Price :
Quantity :
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Shipped with Ice Packs
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Description
CECR1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 490 amino acids (30-511a.a.) and having a molecular mass of 56.9kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CECR1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Insect Cell.
Formulation
CECR1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Adenosine deaminase CECR1 isoform (CECR1) belongs to a family of adenosine deaminase-related growth factors. Adenosine deaminase is a key enzyme of purine nucleotide metabolism. CECR1 is a secreted protein, which is expressed in various tissues, with the highest expression in the lymphoblasts, heart, lung, and the placenta.
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Synonyms
Cat Eye Syndrome Chromosome Region, Candidate 1, Cat Eye Syndrome Critical Region Protein 1, IDGFL, ADA2, ADGF, Adenosine Deaminase 2, EC 3.5.4.4, SNEDS, PAN, CECR1.
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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
IDETRAHLLL KEKMMRLGGR LVLNTKEELA NERLMTLKIA EMKEAMRTLI FPPSMHFFQA KHLIERSQVF NILRMMPKGA ALHLHDIGIV TMDWLVRNVT YRPHCHICFT PRGIMQFRFA HPTPRPSEKC SKWILLEDYR KRVQNVTEFD DSLLRNFTLV TQHPEVIYTN QNVVWSKFET IFFTISGLIH YAPVFRDYVF RSMQEFYEDN VLYMEIRARL LPVYELSGEH HDEEWSVKTY QEVAQKFVET HPEFIGIKII YSDHRSKDVA VIAESIRMAM GLRIKFPTVV AGFDLVGHED TGHSLHDYKE ALMIPAKDGV KLPYFFHAGE TDWQGTSIDR NILDALMLNT TRIGHGFALS KHPAVRTYSW KKDIPIEVCP ISNQVLKLVS DLRNHPVATL MATGHPMVIS SDDPAMFGAK GLSYDFYEVF MGIGGMKADL RTLKQLAMNS IKYSTLLESE KNTFMEIWKK RWDKFIADVA TKLEHHHHHH
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 :
IFIT3 HumanDescription:
IFN-Induced Protein With Tetratricopeptide Repeats 3 Human Recombinant
IFN-Induced Protein With Tetratricopeptide Repeats 3, IFN-Induced Protein With Tetratricopeptide Repeats 4, IFIT4, Retinoic Acid-Induced Gene G Protein, IFN-Induced 60 KDa Protein, IFI-60K, CIG-49, IFIT-3, IFIT-4, ISG-60, CIG49, IFI60, ISG60, RIG-G, P60, GARG-49, IRG2, IFN-induced protein with tetratricopeptide repeats 3.
Product # :
CYT-898Price :
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Description
IFIT3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 513 amino acids (1-490 a.a) and having a molecular mass of 58.4kDa. IFIT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
IFIT3 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
SDS-PAGE
More Info
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Introduction
IFN-Induced Protein With Tetratricopeptide Repeats 3, also known as IFIT3 is a member of the IFIT family. IFN-induced antiviral protein which performs as an inhibitor of cellular and viral processes, cell migration, proliferation, signaling, as well as viral replication. Furthermore, IFIT3 is significantly induced upon RNA virus infection. Ectopic expression or alternatively knockdown of IFIT3 might, respectively, enhance or impair IRF3-mediated gene expression.
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Synonyms
IFN-Induced Protein With Tetratricopeptide Repeats 3, IFN-Induced Protein With Tetratricopeptide Repeats 4, IFIT4, Retinoic Acid-Induced Gene G Protein, IFN-Induced 60 KDa Protein, IFI-60K, CIG-49, IFIT-3, IFIT-4, ISG-60, CIG49, IFI60, ISG60, RIG-G, P60, GARG-49, IRG2, IFN-induced protein with tetratricopeptide repeats 3.
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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 MGSMSEVTKN SLEKILPQLK CHFTWNLFKE DSVSRDLEDR VCNQIEFLNT EFKATMYNLL AYIKHLDGNN EAALECLRQA EELIQQEHAD QAEIRSLVTW GNYAWVYYHL GRLSDAQIYV DKVKQTCKKF SNPYSIEYSE LDCEEGWTQL KCGRNERAKV CFEKALEEKP NNPEFSSGLA IAMYHLDNHP EKQFSTDVLK QAIELSPDNQ YVKVLLGLKL QKMNKEAEGE QFVEEALEKS PCQTDVLRSA AKFYRRKGDL DKAIELFQRV LESTPNNGYL YHQIGCCYKA KVRQMQNTGE SEASGNKEMI EALKQYAMDY SNKALEKGLN PLNAYSDLAE FLETECYQTP FNKEVPDAEK QQSHQRYCNL QKYNGKSEDT AVQHGLEGLS ISKKSTDKEE IKDQPQNVSE NLLPQNAPNY WYLQGLIHKQ NGDLLQAAKC YEKELGRLLR DAPSGIGSIF LSASELEDGS EEMGQGAVSS SPRELLSNSE QLN.
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Background
What is the molecular weight/Mw of IFIT3 HUMAN Protein?
IFIT3 HUMAN Protein has a total Mw of 58.4kDa.
What is the source or expression system of IFIT3 HUMAN Protein?
Escherichia Coli.
What is the Purity of IFIT3 HUMAN Protein?
IFIT3 HUMAN Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of IFIT3 HUMAN Protein?
The biological functionality of IFIT3 HUMAN Protein will be determined in the future.
What is the amino acid sequence of IFIT3 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSMSEVTKN SLEKILPQLK CHFTWNLFKE DSVSRDLEDR VCNQIEFLNT EFKATMYNLL AYIKHLDGNN EAALECLRQA EELIQQEHAD QAEIRSLVTW GNYAWVYYHL GRLSDAQIYV DKVKQTCKKF SNPYSIEYSE LDCEEGWTQL KCGRNERAKV CFEKALEEKP NNPEFSSGLA IAMYHLDNHP EKQFSTDVLK QAIELSPDNQ YVKVLLGLKL QKMNKEAEGE QFVEEALEKS PCQTDVLRSA AKFYRRKGDL DKAIELFQRV LESTPNNGYL YHQIGCCYKA KVRQMQNTGE SEASGNKEMI EALKQYAMDY SNKALEKGLN PLNAYSDLAE FLETECYQTP FNKEVPDAEK QQSHQRYCNL QKYNGKSEDT AVQHGLEGLS ISKKSTDKEE IKDQPQNVSE NLLPQNAPNY WYLQGLIHKQ NGDLLQAAKC YEKELGRLLR DAPSGIGSIF LSASELEDGS EEMGQGAVSS SPRELLSNSE QLN.
What applications can IFIT3 HUMAN Protein be used in?
IFIT3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFIT3 HUMAN Protein?
The endotoxin level is minimal, IFIT3 HUMAN 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 :
Recoverin HumanDescription:
Recoverin Human Recombinant
RCV1, Cancer-associated retinopathy protein, Protein CAR, RCVRN, Recoverin.
Product # :
PRO-441Price :
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Description
Recoverin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids & having a molecular mass of 23kDa.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) contains 20mM Tris-HCl pH 8.0, 1mM EDTA, 2mM MgCl2 and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Recoverin is a member of the recoverin family of neuronal calcium sensors. Recoverin is a heterogeneously acylated calcium-binding and intracellular signal transduction 23kDa protein in the photoreceptor cells of retina. Recoverin contains four EF-hands, of which two bind Ca. Ca-induced extrusion of the acyl group from a hydrophobic cleft in the protein drives the translocation of recoverin from solution to the disc membrane. Recoverin may prolong the termination of the phototransduction cascade in the retina by blocking the phosphorylation of photo-activated rhodopsin. Recoverin plays a key role in the inhibition of rhodopsin kinase, a molecule that regulates the phosphorylation of rhodopsin. This in due course controls the ability of the eye to adapt to, and recover from, exposure to the presence of light. Recoverin is a detectable serologic protein that is expressed in patients with cancer-associated retinopathy, a paraneoplastic syndrome.
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Synonyms
RCV1, Cancer-associated retinopathy protein, Protein CAR, RCVRN, Recoverin.
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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
MGNSKSGALS KEILEELQLN TKFSEEELCS WYQSFLKDCP TGRITQQQFQ SIYAKFFPDT DPKAYAQHVF RSFDSNLDGT LDFKEYVIAL HMTTAGKTNQ KLEWAFSLYD VDGNGTISKNEVLEIVMAIF KMITPEDVKL LPDDENTPEK RAEKIWKYFG KNDDDKLTEK EFIEGTLANK EILRLIQFEP QKVKEKMKNA.
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 :
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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 :
MUSTN1 HumanDescription:
Musculoskeletal, Embryonic Nuclear Protein 1 Human Recombinant
Musculoskeletal, Embryonic Nuclear Protein 1, MUSTANG, Musculoskeletal Embryonic Nuclear Protein 1, Musculoskeletal Temporally Activated Novel, MUSTN1.
Product # :
PRO-2061Price :
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Shipping Method :
Shipped with Ice Packs
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Description
MUSTN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 105 amino acids (1-82 a.a) and having a molecular mass of 11.3kDa. MUSTN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MUSTN1 protein solution (0.25 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Musculoskeletal, Embryonic Nuclear Protein 1, also known as MUSTN1 is a member of the MUSTANG family. MUSTN1 is implicated in the development andregeneration of the musculoskeletal system.
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Synonyms
Musculoskeletal, Embryonic Nuclear Protein 1, MUSTANG, Musculoskeletal Embryonic Nuclear Protein 1, Musculoskeletal Temporally Activated Novel, MUSTN1.
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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 MGSMSQAGAQ EAPIKKKRPP VKEEDLKGAR GNLTKNQEIK SKTYQVMREC EQAGSAAPSV FSRTRTGTET VFEKPKAGPT KSVFG.
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 :
S100A6 HumanDescription:
S100 Calcium Binding Protein A6 Human Recombinant
Protein S100-A6, Calcyclin, Growth factor-inducible protein 2A9, MLN 4, Prolactin receptor-associated protein, PRA, S100 calcium-binding protein A6, S100A6, CACY, 2A9, 5B10, CABP.
Product # :
PRO-148Price :
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Description
S100A6 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 110 amino acids (1-90 a.a.) and having a molecular mass of 12.3kDa. The S100A6 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The S100A6 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 30% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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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 function in stimulation of prolactin secretion and exocytosis. Chromosomal rearrangements and altered expression of the S100A6 gene are implicated in melanoma.
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Synonyms
Protein S100-A6, Calcyclin, Growth factor-inducible protein 2A9, MLN 4, Prolactin receptor-associated protein, PRA, S100 calcium-binding protein A6, S100A6, CACY, 2A9, 5B10, CABP.
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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 MACPLDQAIG LLVAIFHKYS GREGDKHTLS KKELKELIQK ELTIGSKLQD AEIARLMEDL DRNKDQEVNF QEYVTFLGAL ALIYNEALKG.
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 :
SFRP2 MouseDescription:
Secreted Frizzled-Related Protein 2 Mouse Recombinant
Secreted frizzled-related protein 2, sFRP-2, sFRP2, Sfrp2, Protein SDF5, Sdf5, AI851596, sdf, SDF-5, FRP2secreted apoptosis related protein 1, Secreted apoptosis-related protein 1, SARP-1, Sarp1, SARP1.
Product # :
pro-2669Price :
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Description
SFRP2 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 280 amino acids (25-295 a.a) and having a molecular mass of 32.1kDa. SFRP2 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The SFRP2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 20% glycerol and 100mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Secreted frizzled-related protein 2 (SFRP2) belongs to the SFRP family which contains a cysteine-rich domain homologous to the putative Wnt-binding site of Frizzled proteins. SFRP2 functions as soluble modulators of Wnt signaling. Methylation of SFRP2 might indicate on colorectal cancer.
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Synonyms
Secreted frizzled-related protein 2, sFRP-2, sFRP2, Sfrp2, Protein SDF5, Sdf5, AI851596, sdf, SDF-5, FRP2secreted apoptosis related protein 1, Secreted apoptosis-related protein 1, SARP-1, Sarp1, SARP1.
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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
ADPLFLFGQP DFSYKRSNCK PIPANLQLCH GIEYQNMRLP NLLGHETMKE VLEQAGAWIP LVMKQCHPDT KKFLCSLFAP VCLDDLDETI QPCHSLCVQV KDRCAPVMSA FGFPWPDMLE CDRFPQDNDL CIPLASSDHL LPATEEAPKV CEACKTKNED DNDIMETLCK NDFALKIKVK EITYINRDTK IILETKSKTI YKLNGVSERD LKKSVLWLKD SLQCTCEEMN DINAPYLVMG QKQGGELVIT SVKRWQKGQR EFKRISRSIR KLQCHHHHHH
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 :
LXN MouseDescription:
Latexin Mouse Recombinant
Latexin, Endogenous carboxypeptidase inhibitor, ECI, Tissue carboxypeptidase inhibitor, TCI.
Product # :
PRO-2218Price :
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Description
LXN Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 245 amino acids (1-222 a.a) and having a molecular mass of 27.9kDa. LXN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LXN protein solution (1mg/ml) containing Phosphate Buffer Saline (pH7.4), 30% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Lxn also known as Latexin is a member of the protease inhibitor I47 (latexin) family. Lxn's function is hardly reversible, non-competitive, as well as potent inhibitor of CPA1, CPA2 and CPA4. Furthermore, Lxn plays a role in inflammation. Among the diseases associated with LXN are endocervicitis and listeriosis.
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Synonyms
Latexin, Endogenous carboxypeptidase inhibitor, ECI, Tissue carboxypeptidase inhibitor, TCI.
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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 MGSMEIPPTH YAASRAASVA ENCINYQQGT PHKLFLVQTV QQASKEDIPG RGHKYHLKFS VEEIIQKQVT VNCTAEVLYP QMGQGSAPEV NFTFEGEIGK NPDEEDNTFY QSLMSLKRPL EAQDIPDNFG NVSPQMKPVQ HLAWVACGYV MWQNSTEDTW YKMLKIQTVK QVQRNDDFIE LDYTILLHDI ASQEIIPWQM QVLWHPQYGT KVKHNSRLPK EGQAE.
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 :
S.Typhi OMP 52kDaDescription:
Salmonella Typhi Outer Membrane Protein 52kDa Recombinant
Product # :
STY-003Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant S.Typhi OMP produced in E.coli is a non-glycosylated polypeptide chain having a molecular mass of 52 kDa and fused to a His tag at C-terminus.
Source
Escherichia Coli.
Formulation
Lyophilized from 1mg/ml in 20mM sodium carbonate pH-10.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Salmonella Typhi is a pathogen causing typhoid fever, affecting over 17 million people with approximately 600,000 deaths annually worldwide. If untreated, typhoid fever cases result in mortality rates ranging from 12-30%.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized S.Typhi OMP between 2-8°C, do not freeze. Upon reconstitution S.Typhi OMP should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized S.Typhi OMP in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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 :
EFNA1 HumanDescription:
Ephrin A1 Human Recombinant
Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.
Product # :
PRO-971Price :
Quantity :
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Description
EFNA1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 185 amino acids (19-182) and having a molecular mass of 21.6 kDa.EFNA1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The EFNA1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
EFNA1 belongs to the ephrin (EPH) family. The EPH subfamily is the biggest group of receptor protein kinases and they take part in vital nervous system function and development.
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Synonyms
Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.
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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 MDRHTVFWNS SNPKFRNEDY TIHVQLNDYV DIICPHYEDH SVADAAMEQY ILYLVEHEEY QLCQPQSKDQ VRWQCNRPSA KHGPEKLSEK FQRFTPFTLG KEFKEGHSYY YISKPIHQHE DRCLRLKVTV SGKITHSPQA HVNPQEKRLA ADDPEVRVLH SIGHS
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 :
TAX1BP3 HumanDescription:
Tax1 Binding Protein 3 Human Recombinant
Tax1 (human T-cell leukemia virus type I) binding protein 3, TIP-1, Glutaminase-interacting protein 3, Tax interaction protein 1.
Product # :
PRO-981Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TAX1BP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 144 amino acids (1-124 a.a.) and having a molecular mass of 15.8kDa.TAX1BP3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
TAX1BP3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 0.1M NaCl and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
TAX1BP3 holds one PDZ domain, which uses for interactions with other proteins like the interaction with the C-terminus of Rhotekin that facilitates Rho-mediated activation of the FOS serum response element. In addition, PDZ domain interacts with beta-catenin to inhibit the transcriptional activity of beta-catenin. TAX1BP3 exists in several cell lines, such as HeLa, and is expressed in small quantities in peripheral blood leukocytes.
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Synonyms
Tax1 (human T-cell leukemia virus type I) binding protein 3, TIP-1, Glutaminase-interacting protein 3, Tax interaction protein 1.
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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 MSYIPGQPVT AVVQRVEIHK LRQGENLILG FSIGGGIDQD PSQNPFSEDK TDKGIYVTRV SEGGPAEIAG LQIGDKIMQV NGWDMTMVTH DQARKRLTKR SEEVVRLLVT RQSLQKAVQQ SMLS.
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 :
RNF114 HumanDescription:
Ring Finger Protein 114 Human Recombinant
E3 ubiquitin-protein ligase RNF114, RING finger protein 114, Zinc finger protein 228, Zinc finger protein 313, RNF114, ZNF228, ZNF313, PSORS12.
Product # :
PRO-1901Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RNF114 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 251 amino acids (1-228 a.a) and having a molecular mass of 28.1kDa.RNF114 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RNF114 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Ring Finger Protein 114 (RNF114) is expressed in various tissues, including skin, CD4 lymphocytes and dendritic cells. RNF114, which contains 1 RING-type zinc finger, takes part in spermatogenesis.
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Synonyms
E3 ubiquitin-protein ligase RNF114, RING finger protein 114, Zinc finger protein 228, Zinc finger protein 313, RNF114, ZNF228, ZNF313, PSORS12.
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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 MGSMAAQQRD CGGAAQLAGP AAEADPLGRF TCPVCLEVYE KPVQVPCGHV FCSACLQECL KPKKPVCGVC RSALAPGVRA VELERQIEST ETSCHGCRKN FFLSKIRSHV ATCSKYQNYI MEGVKATIKD ASLQPRNVPN RYTFPCPYCP EKNFDQEGLV EHCKLFHSTD TKSVVCPICA SMPWGDPNYR SANFREHIQR RHRFSYDTFV DYDVDEEDMM NQVLQRSIID Q.
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 :
STXBP6 HumanDescription:
Syntaxin Binding Protein 6 Human Recombinant
Syntaxin-binding protein 6, Amisyn, STXBP6, HSPC156, Syntaxin Binding Protein 6.
Product # :
PRO-2056Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
STXBP6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-210 a.a.) and having a molecular mass of 25.9kDa.STXBP6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
STXBP6 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Syntaxin-binding protein 6 (STXBP6) binds components of the SNARE complex and takes part in regulating SNARE complex configuration. STXBP6 forms non-fusogenic complexes with SNAP25 and STX1A and modulates the formation of SNARE complexes and exocytosis.
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Synonyms
Syntaxin-binding protein 6, Amisyn, STXBP6, HSPC156, Syntaxin Binding Protein 6.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSAKSAI SKEIFAPLDE RMLGAVQVKR RTKKKIPFLA TGGQGEYLTY ICLSVTNKKP TQASITKVKQ FEGSTSFVRR SQWMLEQLRQ VNGIDPNGDS AEFDLLFENA FDQWVASTAS EKCTFFQILH HTCQRYLTDR KPEFINCQSK IMGGNSILHS AADSVTSAVQ KASQALNERG ERLGRAEEKT EDLKNSAQQF AETAHKLAMK HKC.
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
More Info
- description
- source
- formulation
- purity
- More Info
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.