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1000 results found for “calreticulin”
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Name :
S100A10 MouseDescription:
Recombinant Mouse S100 Calcium Binding Protein A10
Protein S100-A10, Calpactin I light chain, Calpactin-1 light chain, Cellular ligand of, annexin II, S100 calcium-binding protein A10, p10 protein, p11, S100a10, Cal1l.
Product # :
PRO-2252Price :
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Shipped with Ice Packs
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Description
S100A10 Mouse Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 120 amino acids (1-97a.a) and having a molecular mass of 13.6kDa.S100A10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
S100A10 protein solution (1mg/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
S100A10 is a member of the S100 family of proteins contains two EF-hand calcium-binding motifs and is thought to be involved in the regulation of a number of cellular processes including cell cycle progression and differentiation. 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. S100A10 may function in exocytosis and endocytosis.
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Synonyms
Protein S100-A10, Calpactin I light chain, Calpactin-1 light chain, Cellular ligand of, annexin II, S100 calcium-binding protein A10, p10 protein, p11, S100a10, Cal1l.
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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 MGSMPSQMEH AMETMMLTFH RFAGDKDHLT KEDLRVLMER EFPGFLENQK DPLAVDKIMK DLDQCRDGKV GFQSFLSLVA GLTIACNDYF VVNMKQKGKK.
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 MouseDescription:
Calcium/Calmodulin-Dependent Protein Kinase II Inhibitor 1 Mouse Recombinant
mCaMKIINalpha, calcium/calmodulin-dependent protein kinase II inhibitor alpha, Camk2n1.
Product # :
PKA-092Price :
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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
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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
mCaMKIINalpha, calcium/calmodulin-dependent protein kinase II inhibitor 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 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.
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Name :
FSTL1 HumanDescription:
Follistatin Like 1 Human Recombinant
Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP, Follistatin Like 1, FSL1.
Product # :
CYT-792Price :
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Description
FSTL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 309 amino acids (21-308) and having a molecular mass of 34.9 kDa.FSTL1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The FSTL1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
FSTL1 protein resembles follistatin, an ACTV-binding protein. FSTL1 is an autoantigen associated with rheumatoid arthritis and it holds an FS section, a follistatin-like sequence having 10 conserved cysteine residues.
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Synonyms
Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP, Follistatin Like 1, FSL1.
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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 MEEELRSKSK ICANVFCGAG RECAVTEKGE PTCLCIEQCK PHKRPVCGSN GKTYLNHCEL HRDACLTGSK IQVDYDGHCK EKKSVSPSAS PVVCYQSNRD ELRRRIIQWL EAEIIPDGWF SKGSNYSEIL DKYFKNFDNG DSRLDSSEFL KFVEQNETAI NITTYPDQEN NKLLRGLCVD ALIELSDENA DWKLSFQEFL KCLNPSFNPP EKKCALEDET YADGAETEVD CNRCVCACGN WVCTAMTCDG KNQKGAQTQT EEEMTRYVQE LQKHQETAEK TKRVSTKEI.
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Background
What is the molecular weight/Mw of FSTL1 HUMAN Protein?
FSTL1 HUMAN Protein has a total Mw of 34.9kDa.
What is the source or expression system of FSTL1 HUMAN Protein?
Escherichia Coli.
What is the Purity of FSTL1 HUMAN Protein?
FSTL1 HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of FSTL1 HUMAN Protein?
The biological functionality of FSTL1 HUMAN Protein will be determined in the future.
What is the amino acid sequence of FSTL1 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MEEELRSKSK ICANVFCGAG RECAVTEKGE PTCLCIEQCK PHKRPVCGSN GKTYLNHCEL HRDACLTGSK IQVDYDGHCK EKKSVSPSAS PVVCYQSNRD ELRRRIIQWL EAEIIPDGWF SKGSNYSEIL DKYFKNFDNG DSRLDSSEFL KFVEQNETAI NITTYPDQEN NKLLRGLCVD ALIELSDENA DWKLSFQEFL KCLNPSFNPP EKKCALEDET YADGAETEVD CNRCVCACGN WVCTAMTCDG KNQKGAQTQT EEEMTRYVQE LQKHQETAEK TKRVSTKEI.
What applications can FSTL1 HUMAN Protein be used in?
FSTL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FSTL1 HUMAN Protein?
The endotoxin level is minimal, FSTL1 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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Description:
Vasoactive Intestinal Peptide
Product # :
HOR-043Price :
Quantity :
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Shipped at Room temp
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Description
Vasoactive Intestinal Peptide Synthetic is a single, non-glycosylated polypeptide chain containing 28 amino acids, having a molecular mass of 3325 Dalton and a Molecular formula of C147H238N44O42S .
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Vasoactive Intestinal Peptide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Vasoactive Intestinal Peptide 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 Vasoactive Intestinal Peptide in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
H-His-Ser-Asp-Ala-Val-Phe-Thr-Asp-Asn-Tyr-Thr-Arg-Leu-Arg-Lys-Gln-Met-Ala-Val-Lys-Lys-Tyr-Leu-Asn-Ser-Ile-Leu-Asn-NH2.
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Background
Vasoactive Intestinal Peptide (VIP), a prominent member of the glucagon-secretin peptide superfamily, plays a multifaceted role as a neuropeptide and neurotransmitter. This research paper aims to provide an extensive analysis of VIP, exploring its biochemical properties, diverse physiological functions, and potential therapeutic applications in various disease conditions.
Vasoactive Intestinal Peptide (VIP), originally identified for its potent vasodilatory properties in the gastrointestinal system, has since been recognized for its wide-ranging physiological effects throughout the body. As a neuropeptide and neurotransmitter.
VIP, a 28-amino acid peptide, exhibits a diverse range of biological activities due to its interactions with multiple G protein-coupled receptors (GPCRs) from the VIP/PACAP receptor family (Harmar et al., 2012). These receptors are expressed in various tissues and cells, enabling VIP to exert its pleiotropic effects.
VIP is involved in the regulation of numerous physiological processes. It functions as a potent vasodilator, modulates smooth muscle activity in the gastrointestinal tract, and participates in neurotransmission in the central and peripheral nervous systems (Lelievre et al., 2008). Additionally, VIP has immunomodulatory properties, influencing immune cell functions and inflammatory responses (Delgado et al., 2004).
VIP serves as a neurotransmitter in the central nervous system, where it contributes to various neuronal functions, including learning, memory, and sensory perception (Deng et al., 2015). Moreover, VIP has demonstrated neuroprotective effects in neurodegenerative disorders, making it a potential therapeutic target for neuroprotection and neuroregeneration (Delgado et al., 2002).
VIP's diverse physiological functions offer potential therapeutic applications in various disease contexts. Research has explored its potential in the treatment of inflammatory diseases, neurodegenerative disorders, and gastrointestinal disorders (Delgado et al., 2013). Furthermore, VIP-based therapies are being investigated for their neuroprotective potential in brain injuries and stroke.
As the research on VIP continues to progress, further investigation is warranted to uncover the precise mechanisms of action and potential clinical applications in medicine. VIP stands as a remarkable example of a neuropeptide with extensive physiological roles and therapeutic potential in various disease conditions.
What is the molecular weight/Mw of VASOACTIVE INTESTINAL PEPTIDE Protein?
VASOACTIVE INTESTINAL PEPTIDE Protein has a total Mw of 3.32kDa.
What is the Purity of VASOACTIVE INTESTINAL PEPTIDE Protein?
VASOACTIVE INTESTINAL PEPTIDE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of VASOACTIVE INTESTINAL PEPTIDE Protein?
The biological functionality of VASOACTIVE INTESTINAL PEPTIDE Protein will be determined in the future.
What is the amino acid sequence of VASOACTIVE INTESTINAL PEPTIDE Protein?
H-His-Ser-Asp-Ala-Val-Phe-Thr-Asp-Asn-Tyr-Thr-Arg-Leu-Arg-Lys-Gln-Met-Ala-Val-Lys-Lys-Tyr-Leu-Asn-Ser-Ile-Leu-Asn-NH2.
What applications can VASOACTIVE INTESTINAL PEPTIDE Protein be used in?
VASOACTIVE INTESTINAL PEPTIDE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for VASOACTIVE INTESTINAL PEPTIDE Protein?
The endotoxin level is minimal, VASOACTIVE INTESTINAL PEPTIDE 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 :
ARTN HumanDescription:
Artemin Human Recombinant
ART, ARTN , EVN, NBN.
Product # :
CYT-306Price :
Quantity :
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Shipped at Room temp
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Description
Artemin Human Recombinant produced in E.Coli is a disulfide-linked homodimer, non-glycosylated, polypeptide chain containing 2 x 113 amino acids and having a total molecular mass of 24.2 kDa. Artemin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Artemin was lyophilized after extensive dialysis against 10mM sodium citrate pH-4.5 and 25mM sodium chloride.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is determined by the dose-dependent proliferation of the SH-SY5Y cell line and is typically 4-8 ng/mL. The activity can also be determined by its ability to promote survival and neurite outgrowth.More Info
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Introduction
The protein encoded by this gene is a member of the glial cell line-derived neurotophic factor (GDNF) family of ligands which are a group of ligands within the TGF-beta superfamily of signaling molecules. GDNFs are unique in having neurotrophic properties and have potential use for gene therapy in neurodegenrative disease. Artemin has been shown in culture to support the survival of a number of periferal neuron populations and at least one population of dopaminergic CNS neurons. Its role in the PNS and CNS is further substantiated by its expression pattern in the proximity of these neurons. This protein is a ligand for the RET receptor and uses GFR-alpha 3 as a coreceptor. Four alternatively spliced transcripts have been described, two of which encode the same protein.
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Synonyms
ART, ARTN , EVN, NBN.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Artemin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Artemin Human Recombinant 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 Artemin 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
AGGPGSRARA AGARGCRLRS QLVPVRALGL GHRSDELVRF RFCSGSCRRA RSPHDLSLAS LLGAGALRPP PGSRPVSQPC CRPTRYEAVS FMDVNSTWRT VDRLSATACG CLG.
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Background
Artemin Human Recombinant: Unraveling its Role in Neurobiology and Therapeutic Applications
Abstract:
Artemin, a member of the glial cell line-derived neurotrophic factor (GDNF) family, holds significant potential in neurobiology and therapeutic interventions. This research paper provides an overview of Artemin human recombinant, elucidating its molecular characteristics, signaling pathways, and therapeutic implications in neurological disorders. Understanding the multifaceted role of Artemin offers new avenues for targeted therapies. This article offers a concise analysis of Artemin, highlighting its impact on neurobiology and its therapeutic applications.
Introduction:
Neurological disorders represent a major challenge in healthcare, necessitating innovative therapeutic strategies. Artemin, a member of the GDNF family, has emerged as a promising molecule in neurobiology. This paper provides an overview of Artemin, shedding light on its structure, function, and therapeutic potential.
Artemin Signaling and Mechanisms:
Artemin binds to its receptor, Ret tyrosine kinase, and activates downstream signaling pathways, including the PI3K/AKT and MAPK pathways. These signaling cascades play crucial roles in neuronal survival, growth, and differentiation, highlighting the significance of Artemin in neurodevelopment and neuroprotection.
Artemin in Neurological Disorders:
Artemin has been implicated in various neurological disorders, including peripheral neuropathies and neurodegenerative diseases. Its neuroprotective properties and ability to enhance neuronal survival and regeneration make it a promising target for therapeutic interventions. Furthermore, Artemin may play a role in pain modulation and sensory neuron function.
Therapeutic Potential of Artemin Human Recombinant:
Artemin human recombinant offers promising prospects in the field of neurotherapeutics. Strategies aimed at modulating Artemin signaling or delivering exogenous Artemin hold potential for promoting neuronal survival, regeneration, and functional recovery. Artemin-based therapies could be developed for a range of neurological disorders, including peripheral neuropathies, Parkinson's disease, and spinal cord injuries.
Challenges and Future Directions:
While the therapeutic targeting of Artemin shows promise, several challenges lie ahead. Further research is needed to understand the precise mechanisms underlying Artemin's effects and its interactions with other signaling pathways. Additionally, the development of effective delivery methods and the identification of patient subgroups that may benefit from Artemin-based therapies are important considerations for clinical translation.
Conclusion:
Artemin human recombinant represents a promising avenue for therapeutic interventions in neurological disorders. Understanding the molecular mechanisms and functional implications of Artemin in neurobiology offers new opportunities for developing innovative treatments. Continued research in this field has the potential to improve the lives of individuals affected by neurological conditions and advance the field of neurotherapeutics.
What is the molecular weight/Mw of ARTN Protein?
ARTN Protein has a total Mw of 24.2kDa.
What is the source or expression system of ARTN Protein?
Escherichia Coli.
What is the Purity of ARTN Protein?
ARTN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of ARTN Protein?
The activity is determined by the dose-dependent proliferation of the SH-SY5Y cell line and is typically 4-8 ng/mL. The activity can also be determined by its ability to promote survival and neurite outgrowth.
What is the amino acid sequence of ARTN Protein?
AGGPGSRARA AGARGCRLRS QLVPVRALGL GHRSDELVRF RFCSGSCRRA RSPHDLSLAS LLGAGALRPP PGSRPVSQPC CRPTRYEAVS FMDVNSTWRT VDRLSATACG CLG.
What applications can ARTN Protein be used in?
ARTN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ARTN Protein?
The endotoxin level is minimal, ARTN 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 :
GRPEL1 HumanDescription:
GrpE-Like 1 Human Recombinant
HMGE, GrpE-like protein cochaperone, GREPEL1, FLJ25609.
Product # :
PRO-263Price :
Quantity :
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Shipped with Ice Packs
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Description
GRPEL1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids (28-217a.a.) and having a molecular mass of 23.6kDa.GRPEL1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GRPEL1 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
GRPEL1 is a vital component of the PAM complex, a complex necessary for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. GRPEL1 protein controls the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins.
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Synonyms
HMGE, GrpE-like protein cochaperone, GREPEL1, FLJ25609.
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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 MCTATKQKNS GQNLEEDMGQ SEQKADPPAT EKTLLEEKVK LEEQLKETVE KYKRALADTE NLRQRSQKLV EEAKLYGIQA FCKDLLEVAD VLEKATQCVP KEEIKDDNPH LKNLYEGLVM TEVQIQKVFT KHGLLKLNPV GAKFDPYEHE ALFHTPVEGK EPGTVALVSK VGYKLHGRTL RPALVGVVKE 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 :
AAMDC HumanDescription:
Adipogenesis Associated, Mth938 Domain Containing Human Recombinant
Adipogenesis Associated, Mth938 Domain Containing, Adipogenesis Associated Mth938 Domain-Containing Protein , C11orf67, Chromosome 11 Open Reading Frame 67, Mth938 Domain-Containing Protein, UPF0366 Protein C11orf67, PTD015, CK067,AAMDC.
Product # :
PRO-2116Price :
Quantity :
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Shipped with Ice Packs
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Description
AAMDC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 145 amino acids (1-122 a.a) and having a molecular mass of 15.7 kDa.AAMDC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AAMDC protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Adipogenesis Associated, Mth938 Domain Containing, also known as AAMDC is a member of the AAMDC family and takes part in preadipocyte differentiation andadipogenesis.
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Synonyms
Adipogenesis Associated, Mth938 Domain Containing, Adipogenesis Associated Mth938 Domain-Containing Protein , C11orf67, Chromosome 11 Open Reading Frame 67, Mth938 Domain-Containing Protein, UPF0366 Protein C11orf67, PTD015, CK067,AAMDC.
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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 MGSMTSPEIA SLSWGQMKVK GSNTTYKDCK VWPGGSRTWD WRETGTEHSP GVQPADVKEV VEKGVQTLVI GRGMSEALKV PSSTVEYLKK HGIDVRVLQT EQAVKEYNAL VAQGVRVGGV FHSTC.
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 :
ARPC3 HumanDescription:
Actin Related Protein 2/3 Complex, Subunit 3 Human Recombinant
ARC21, p21-Arc, Actin-related protein 2/3 complex subunit 3, Arp2/3 complex 21 kDa subunit, ARPC3.
Product # :
PRO-1413Price :
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Description
ARPC3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-178 a.a) and having a molecular mass of 22.9kDa. ARPC3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
ARPC3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Actin-related protein 2/3 complex subunit 3 (ARPC3) which Belongs to the ARPC3 family is one of 7 subunits of the human Arp2/3 protein complex. The Arp2/3 complex is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. ARPC3 which is localized to the cytoplasm and cytoskeleton, interacts with p20-ARC and takes part in the structural integrity of the protein complex.
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Synonyms
ARC21, p21-Arc, Actin-related protein 2/3 complex subunit 3, Arp2/3 complex 21 kDa subunit, ARPC3.
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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 MGSMPAYHSS LMDPDTKLIG NMALLPIRSQ FKGPAPRETK DTDIVDEAIY YFKANVFFKN YEIKNEADRT LIYITLYISE CLKKLQKCNS KSQGEKEMYT LGITNFPIPG EPGFPLNAIY AKPANKQEDE VMRAYLQQLR QETGLRLCEK VFDPQNDKPS KWWTCFVKRQ FMNKSLSGPG 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 :
SNTN HumanDescription:
Sentan Cilia Apical Structure Protein Human Recombinant
Sentan cilia apical structure protein, FLJ44379, S100AL, S100A1L, S100A-like protein, sentan, S100 calcium-binding protein A1-like.
Product # :
PRO-216Price :
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Shipping Method :
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Description
SNTN 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 167 amino acids (1-147a.a.) and having a molecular mass of 18.6kDa. The SNTN is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SNTN solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50% glycerol and 0.15M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
SNTN is a member of to the S-100 family. SNTN is localized solely to the bridging structure between the cell membrane and peripheral singlet microtubules that specifically exists in the narrowed distal portion of cilia. Exogenously expressed sentan displayed affinity for the membrane protrusions, and a protein-lipid binding assay discovered that sentan bounds to phosphatidylserine which indicate that sentan is the leading molecular component of the ciliary tip to link the cell membrane and peripheral singlet microtubules, making the distal portion of the cilia narrow and stiff to permit better airway approval or ovum transport.
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Synonyms
Sentan cilia apical structure protein, FLJ44379, S100AL, S100A1L, S100A-like protein, sentan, S100 calcium-binding protein A1-like.
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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 MGGCMHSTQD KSLHLEGDPN PSAAPTSTCA PRKMPKRISI SKQLASVKAL RKCSDLEKAI ATTALIFRNS SDSDGKLEKA IAKDLLQTQF RNFAEGQETK PKYREILSEL DEHTENKLDF EDFMILLLSI TVMSDLLQNI RNVKIMK
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 :
EREG Human, HisDescription:
Epiregulin Human Recombinant, His Tag
Epiregulin, Proepiregulin, ER, ERP.
Product # :
CYT-859Price :
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- sds-page
Description
EREG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 69 amino acids (63-108 a.a) and having a molecular mass of 7.7kDa. EREG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EREG protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE
sds-page
More Info
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Introduction
Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence.
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Synonyms
Epiregulin, Proepiregulin, ER, ERP.
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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 MGSVSITKCS SDMNGYCLHG QCIYLVDMSQ NYCRCEVGYT GVRCEHFFL.
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Background
What is the molecular weight/Mw of EREG Protein?
EREG Protein has a total Mw of 7.7kDa.
What is the source or expression system of EREG Protein?
Escherichia Coli.
What is the Purity of EREG Protein?
EREG Protein is >80% pure as determined by SDS-PAGE.
What is the Biological Activity of EREG Protein?
The biological functionality of EREG Protein will be determined in the future.
What is the amino acid sequence of EREG Protein?
MGSSHHHHHH SSGLVPRGSH MGSVSITKCS SDMNGYCLHG QCIYLVDMSQ NYCRCEVGYT GVRCEHFFL.
What applications can EREG Protein be used in?
EREG Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EREG Protein?
The endotoxin level is minimal, EREG 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 :
TCL1A HumanDescription:
T-cell Leukemia/Lymphoma 1A Human Recombinant
T-cell leukemia/lymphoma protein 1A, Protein p14 TCL1, Oncogene TCL-1, Oncogene TCL1, TCL1A, TCL1.
Product # :
PRO-726Price :
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Description
TCL1A Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 114 amino acids (1-114 a.a.) and having a molecular mass of 13.4kDa.The TCL1A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TCL1A protein solution contains 50mM Tris-HCl buffer (pH7.5) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
TCL1A (T-cell leukemia/lymphoma 1A) is a protein with a possible role in intracellular regulation of T cell signaling. TCL1A enhances cell proliferation, stabilizes mitochondrial membrane potential and promotes cell survival. TCL1A is restricted in the T-cell lineage to immature thymocytes and activated peripheral lymphocytes. TCL1A is preferentially expressed early in T and B-lymphocyte differentiation. Chromosomal anomalies activating TCL1A are found in chronic T-cell leukemias (T-CLL).
TCL1A enhances the phosphorylation and activation of AKT1, AKT2 and AKT3. TCL1A promotes nuclear translocation of AKT1. TCL1A binds to the pleckstrin homology domain of Akt (protein kinase B) family proteins, which facilitates Akt dimerization and activity. By increasing Akt activity, TCL1A can enhance the serine/threonine phosphorylation of major Akt signaling substrates, for example Ikk complex, mTOR, BAD, p70S6 kinase, FOXO transcription factors and GSK3b. These substrates regulate cellular differentiation, growth, survival, and metabolism. -
Synonyms
T-cell leukemia/lymphoma protein 1A, Protein p14 TCL1, Oncogene TCL-1, Oncogene TCL1, TCL1A, TCL1.
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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
MAECPTLGEA VTDHPDRLWA WEKFVYLDEK QHAWLPLTIE IKDRLQLRVL LRREDVVLGR PMTPTQIGPS LLPIMWQLYP DGRYRSSDSS FWRLVYHIKI DGVEDMLLEL LPDD.
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 :
KRT16 HumanDescription:
Cytokeratin 16 Human Recombinant
Keratin, type I cytoskeletal 16, Cytokeratin 16, KRT16, Cytokeratin-16, CK-16, Keratin-16, K16, KRT16A, FNEPPK, K1CP, NEPPK.
Product # :
PRO-1899Price :
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Description
KRT16 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 496 amino acids (1-473) and having a molecular mass of 53.7 kDa.KRT16 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The KRT16 solution (1mg/ml) contains 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
Cytokeratin 16, also known as KRT16, is a member of the keratin gene family. KRT16 which acts as a regulator of innate immunity in response to skin barrier breach is required for some inflammatory checkpoint for the skin barrier maintenance. KRT16 is coexpressed with keratin 14 in a few epithelial tissues as esophagus, tongue, and hair follicles.
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Synonyms
Keratin, type I cytoskeletal 16, Cytokeratin 16, KRT16, Cytokeratin-16, CK-16, Keratin-16, K16, KRT16A, FNEPPK, K1CP, NEPPK.
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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 MGSMTTCSRQ FTSSSSMKGS CGIGGGIGGG SSRISSVLAG GSCRAPSTYG GGLSVSSRFS SGGACGLGGG YGGGFSSSSS FGSGFGGGYG GGLGAGFGGG LGAGFGGGFA GGDGLLVGSE KVTMQNLNDR LASYLDKVRA LEEANADLEV KIRDWYQRQR PSEIKDYSPY FKTIEDLRNK IIAATIENAQ PILQIDNARL AADDFRTKYE HELALRQTVE ADVNGLRRVL DELTLARTDL EMQIEGLKEE LAYLRKNHEE EMLALRGQTG GDVNVEMDAA PGVDLSRILN EMRDQYEQMA EKNRRDAETW FLSKTEELNK EVASNSELVQ SSRSEVTELR RVLQGLEIEL QSQLSMKASL ENSLEETKGR YCMQLSQIQG LIGSVEEQLA QLRCEMEQQS QEYQILLDVK TRLEQEIATY RRLLEGEDAH LSSQQASGQS YSSREVFTSS SSSSSRQTRP ILKEQSSSSF SQGQSS.
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 :
CDC37 HumanDescription:
Cell Division Cycle 37 Human Recombinant
P50CDC37, CDC-37, CDC37, Hsp90 co-chaperone Cdc37, Hsp90 chaperone protein kinase-targeting subunit, CDC37A, Cell Division Cycle 37.
Product # :
PRO-464Price :
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Description
CDC37 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 378 amino acids and having a molecular mass of 44.4 kDa.
Source
Escherichia Coli.
Formulation
The CDC37 protein solution contains 20mM Tris-HCl pH-8 & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CDC37 is an essential protein in Saccharomyces cerevisiae and is a molecular chaperone with precise function in cell signal transduction. CDC37 forms a complex/associates with Hsp90 molecular chaperone as one of several auxiliary proteins that are collectively referred to as Hsp90 co-chaperones. CDC37 also forms complex with a number of protein kinases such as CDK4, CDK6, SRC, RAF-1, MOK, as well as eIF2 alpha kinases. CDC34 is involved in directing Hsp90 to its target kinases. CDC37 up-regulation is a common early event in some localized human cancers. CDC37 is necessary for maintaining prostate tumor cell growth and represents a novel target in the exploration for multitargeted therapies. CDC37 plays a role in regulating Hsp90 ATPase activity. CDC37 binds to Akt and HSP90 in the signal transduction pathway in human tumor cells. Tnf-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90. CDC37 and heat shock protein 90 bind specifically to the kinase domain of LKB1.
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Synonyms
P50CDC37, CDC-37, CDC37, Hsp90 co-chaperone Cdc37, Hsp90 chaperone protein kinase-targeting subunit, CDC37A, Cell Division Cycle 37.
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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
MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DRGCRECKRK VAECQRKLKE LEVAEGGKAE LERLQAEAQQ LRKEERSWEQ KLEEMRKKEK SMPWNVDTLS KDGFSKSMVN TKPEKTEEDS EEVREQKHKT FVEKYEKQIK HFGMLRRWDD SQKYLSDNVH LVCEETANYL VIWCIDLEVE EKCALMEQVA HQTIVMQFIL ELAKSLKVDP RACFRQFFTK IKTADRQYME GFNDELEAFK ERVRGRAKLR IEKAMKEYEE EERKKRLGPG GLDPVEVYES LPEELQKCFD VKDVQMLQDA ISKMDPTDAK YHMQRCIDSG LWVPNSKASE AKEGEEAGPG DPLLEAVPKT GDEKDVSV.
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 :
GHRL HumanDescription:
Ghrelin Human Recombinant
Appetite-regulating hormone precursor, Growth hormone secretagogue, Growth hormone-releasing peptide, GHRP, Motilin-related peptide, M46 protein, Ghrelin, Obestatin, MTLRP.
Product # :
HOR-294Price :
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Description
Ghrelin Human Recombinant contains 115 amino acids (24-117 a.a.) and a total molecular mass of 12.8 kDa. The GHRL is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Ghrelin protein solution contains 20mM Tris-HCl, pH-8 & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Obestatin is a hormone that is produced in the cells lining the stomach and small intestine of several mammals including humans; it drastically reduces appetite in mice and is expected to do the same in humans. Obestatin is a peptide hormone - a relatively small protein. It is encoded by the same gene that also encodes ghrelin, a peptide hormone that increases appetite. The protein produced by that gene breaks into two smaller peptides, ghrelin and obestatin. Ghrelin is an endogenous ligand for the growth hormone secretagogue receptor and is involved in regulating growth hormone release. Ghrelin is derived from a preprohormone called preproghrelin, which also generates a second peptide called obestatin. Ghrelin is an endogenous ligand for the orphan G protein-coupled receptor GPR39 and is involved in satiety and decreased food intake.
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Synonyms
Appetite-regulating hormone precursor, Growth hormone secretagogue, Growth hormone-releasing peptide, GHRP, Motilin-related peptide, M46 protein, Ghrelin, Obestatin, MTLRP.
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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 MGSSFLSPEH QRVQQRKESK KPPAKLQPRA LAGWLRPEDG GQAEGAEDEM EVRFNAPFDV GIKLSGVQYQ QHSQALGKFL QDILWEEAKE APADK.
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Background
What is the molecular weight/Mw of GHRELIN HUMAN Protein?
GHRELIN HUMAN Protein has a total Mw of 12.8kDa.
What is the source or expression system of GHRELIN HUMAN Protein?
Escherichia Coli.
What is the Purity of GHRELIN HUMAN Protein?
GHRELIN HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of GHRELIN HUMAN Protein?
The biological functionality of GHRELIN HUMAN Protein will be determined in the future.
What is the amino acid sequence of GHRELIN HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSSFLSPEH QRVQQRKESK KPPAKLQPRA LAGWLRPEDG GQAEGAEDEM EVRFNAPFDV GIKLSGVQYQ QHSQALGKFL QDILWEEAKE APADK.
What applications can GHRELIN HUMAN Protein be used in?
GHRELIN HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GHRELIN HUMAN Protein?
The endotoxin level is minimal, GHRELIN 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 :
CFL2 HumanDescription:
Cofilin-2 Human Recombinant
Cofilin-2, Cofilin- muscle isoform, CFL2, NEM7.
Product # :
PRO-912Price :
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Description
CFL2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 186 amino acids (1-166 a.a.) and having a molecular mass of 20.9kDa.CFL2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CFL2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 50mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CFL2 protein is a member of the actin-binding proteins ADF family which contains 1 ADF-H domain. Cofilin is a broadly distributed intracellular actin-modulating protein which binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. Defects in the CFL2 gene are the cause of nemaline myopathy type 7 (NEM7).
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Synonyms
Cofilin-2, Cofilin- muscle isoform, CFL2, NEM7.
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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 MASGVTVNDE VIKVFNDMKV RKSSTQEEIK KRKKAVLFCL SDDKRQIIVE EAKQILVGDI GDTVEDPYTS FVKLLPLNDC RYALYDATYE TKESKKEDLV FIFWAPESAP LKSKMIYASS KDAIKKKFTG IKHEWQVNGL DDIKDRSTLG EKLGGNVVVS LEGKPL.
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 :
PSMD10 HumanDescription:
Gankyrin Human Recombinant
26S proteasome non-ATPase regulatory subunit 10, 26S proteasome regulatory subunit p28, Gankyrin, PSMD10, p28, dJ889N15.2.
Product # :
ENZ-404Price :
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Shipped with Ice Packs
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Description
PSMD10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 226 amino acids and having a molecular mass of 24.4 kDa.
Source
Escherichia Coli.
Formulation
The PSMD10 protein solution (1mg/ml) contains 1x PBS pH-7.4 & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Gankyrin (proteasome 26S subunit) is a multicatalytic proteinase oncoprotein commonly overexpressed in most hepatocellular carcinomas. Proteasomes are found throughout eukaryotic cells at a high concentrations and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. Gankyrin interacts with S6 ATPase of the 19S regulatory particle of the 26S proteasome. Gankyrin is involved in theregulation of the phosphorylation of the retinoblastoma protein by CDK4, and to enhance the ubiquitinylation of p53 by MDM2. Gankyrin consists of 7 ankyrin repeats and is structurally similar to I kappa Bs. Gankyrin acts as a regulatory subunit of the 26s proteasome which is involved in the atp-dependent degradation of ubiquitinated proteins. Gankyrin is involved in progression of esophageal squamous cell carcinoma. gankyrin plays an oncogenic role especially in early stages of human epatocarcinogenesis. Gankyrin binds to NF-kappaB and suppresses its activity at the transcription level by modulating acetylation through SIRT1. Structural comparison between Gankyrin & p16(INK4A) identified numerous residues of gankyrin that are potentially important for CDK4 binding.
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Synonyms
26S proteasome non-ATPase regulatory subunit 10, 26S proteasome regulatory subunit p28, Gankyrin, PSMD10, p28, dJ889N15.2.
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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
MEGCVSNLMV CNLAYSGKLE ELKESILADK SLATRTDQDS RTALHWACSA GHTEIVEFLL QLGVPVNDKD DAGWSPLHIA ASAGRDEIVK ALLGKGAQVN AVNQNGCTPL HYAASKNRHE IAVMLLEGGA NPDAKDHYEA TAMHRAAAKG NLKMIHILLY YKASTNIQDT EGNTPLHLAC DEERVEEAKL LVSQGASIYI ENKEEKTPLQ VAKGGLGLIL KRMVEG.
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 :
VAMP3 HumanDescription:
Synaptobrevin-3 Human Recombinant
VAMP3, VAMP-3, Cellubrevin, Vesicle-Associated Membrane Protein 3, Synaptobrevin-3, CEB, SYB3.
Product # :
PRO-652Price :
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Description
VAMP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8.7 kDa.
Source
Escherichia Coli.
Formulation
The VAMP3 protein solution contains 20mM Tris pH-7.5 and 10% glycerol.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
VAMP3 is present in recycling endosomes and endosome-derived vesicles. VAMP3 has been implicated in recycling of transferrin receptors to the plasma membrane, secretion of alpha-granules in platelets, recycling of T-cell receptors to the immunological synapses, and membrane trafficking during cell migration. VAMP-3 is present in human platelets and necessary for granule secretion. Synaptobrevins are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. VAMP3 high homology to other VAMPs in its broad tissue distribution and subcellular localization is shown to be the human equivalent of the rodent cellubrevin. In platelets the protein resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation.
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Synonyms
VAMP3, VAMP-3, Cellubrevin, Vesicle-Associated Membrane Protein 3, Synaptobrevin-3, CEB, SYB3.
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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
MSTGPTAATG SNRRLQQTQN QVDEVVDIMR VNVDKVLERD QKLSELDDRA DALQAGASQF ETSAAKLKRK YWWKNCK.
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 :
CAPNS1 AntibodyDescription:
Calpain, Small Subunit 1, Mouse Anti Human
Calpain Small Subunit 1, CAPN4, Calcium-Activated Neutral Proteinase Small Subunit, Calcium-Dependent Protease Small Subunit 1, Calpain Regulatory Subunit, CANP Small Subunit, CDPS, CSS1, Calcium-Dependent Protease Small Subunit, Calcium-Dependent Protease Small Subunit, Calpain 4 Small Subunit (30K), Calpain Small Polypeptide, Calpain Small Subunit 1, CALPAIN4, CANPS, CAPNS, CANP, CAPNS1.
Product # :
ANT-587Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
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Introduction
Calpain, Small Subunit 1 (CAPNS1) belongs to the calpain small subunit family. Calpains are a ubiquitous, well-conserved family of calcium-dependent, cysteine proteases, widely distributed in mammalian cells. Calpain families are implicated in neurodegenerative processes, considering that their activation can be triggered by calcium influx and oxidative stress. Calpains function as heterodimers, comprising a specific large catalytic subunit (calpain 1 subunit in Calpain I, and calpain 2 subunit in Calpain II), and a common small regulatory subunit encoded by the CAPNS1 gene. The CAPNS1 protein is vital for the stability and function of both calpain heterodimers, whose proteolytic activities influence numerous cellular functions including apoptosis, proliferation, migration, adhesion, and autophagy.
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Synonyms
Calpain Small Subunit 1, CAPN4, Calcium-Activated Neutral Proteinase Small Subunit, Calcium-Dependent Protease Small Subunit 1, Calpain Regulatory Subunit, CANP Small Subunit, CDPS, CSS1, Calcium-Dependent Protease Small Subunit, Calcium-Dependent Protease Small Subunit, Calpain 4 Small Subunit (30K), Calpain Small Polypeptide, Calpain Small Subunit 1, CALPAIN4, CANPS, CAPNS, CANP, CAPNS1.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human CAPNS1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human CAPNS1 protein 84-268 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and k light chain.
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Clone
PAT1D11AT.
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Applications
CAPNS1 antibody has been tested by ELISA, Western blot analysis, ICC/IF and Flow cytometry to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
CAPNS1 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
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 :
ctxBDescription:
Cholera Toxin B subunit Recombinant
Cholera enterotoxin subunit B, Cholera enterotoxin B chain, Cholera enterotoxin gamma chain, Choleragenoid, ctxB, toxB.
Product # :
PRO-2605Price :
Quantity :
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Shipped with Ice Packs
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Description
Cholera Toxin B subunit Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 103 amino acids and having a molecular mass of 11.6kDa.ctxB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ctxB is supplied as a 0.2 μm filtered solution conteining 5mM PB, pH 7.0, 75mM NaCl, and 50 % glycerol.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Cholera Toxin B subunit (ctxB) Cholera is a protein complex secreted by the bacterium Vibrio cholerae. ctxB is responsible for the massive, watery diarrhea characteristic of cholera infection. The cholera toxin is an oligomeric complex made up of 6 protein subunits: a single copy of the A subunit and5 copies of the B subunit, denoted as AB5. Subunit B binds while subunit A activates the G protein which activates adenylate cyclase. The five B subunits form a five-membered ring. The A subunit has 2 important segments. The A1 portion of the chain (CTA1) is a globular enzyme payload that ADP-ribosylates G proteins, while the A2 chain (CTA2) forms an extended alpha helix which sits snugly in the central pore of the B subunit ring.
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Synonyms
Cholera enterotoxin subunit B, Cholera enterotoxin B chain, Cholera enterotoxin gamma chain, Choleragenoid, ctxB, toxB.
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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
TPQNITDLCA EYHNTQIYTL NDKIFSYTES LAGKREMAII TFKNGAIFQV EVPGSQHIDS QKKAIERMKD TLRIAYLTEA KVEKLCVWNN KTPHAIAAIS MAN.
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 :
Activin-A Human Plant-ActiveDescription:
Activin-A Human Recombinant, Plant-Active
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-414Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Active form Activin-A Human Recombinant produced in Plant is a homodimeric, glycosylated, polypeptide chain containing 2 x 116 amino acids and having a molecular weight of 27.4kDa.The Active form Activin-A is fused to a 6-His tag at N-terminus and purified by standard chromatographic techniques.
Source
Nicotiana benthamiana.
Formulation
Active form Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 50mM Tris-HCl pH-7.4
Purity
Greater than 98% as obsereved by SDS-PAGE.
Biological Activity
The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.More Info
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Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Lyophilized freeze dried powder.
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Stability
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Repeated freezing and thawing is not recommended.
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Solubility
INHBA protein should be reconstituted in distilled water to a concentration of 50 ug /ml. Due to the protein nature, dimmers and multimers may be observed.
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Amino Acid Sequence
HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSG
YHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFA
NLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS. -
Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 27.4 kDa.What is the source or expression system of Activin A Protein?
Nicotiana benthamiana.What is the Purity of Activin A Protein?
Activin A Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin A Protein?
The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.What is the endotoxin level for Activin A Protein?
The endotoxin level is minimal, ACTIVIN A Protein was purified using conventional chromatography techniques.What is the amino acid sequence of ACTIVIN A Protein?HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS
What applications can ACTIVIN-A Protein be used in?
ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.
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 :
CCL20 Human, HisDescription:
Macrophage Inflammatory protein-3 alpha (CCL20) Human Recombinant, His Tag
S Small inducible cytokine A20 precursor, CCL20, Macrophage inflammatory protein 3 alpha, MIP-3-alpha, Liver and activation- regulated chemokine, CC chemokine LARC, Beta chemokine exodus-1, CKb4, LARC, ST38, MIP3A, MIP-3a, SCYA20.
Product # :
CHM-252Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
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- More Info
Description
MIP 3a Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 91 amino acids (27-96 a.a.) and having a molecular mass of 10.3kDa. The MIP 3a is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MIP 3a solution (0.25 mg/ml) contains Phosphate Buffered Saline pH7.4 and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
CCL-20 is a chemotactic factor that draws lymphocytes & neutrophils, rathar than monocytes. MIP-3 alpha inhibits proliferation of myeloid progenitors in colony formation assays. MIP3A plays a role in the formation and function of the mucosal lymphoid tissues by attracting lymphocytes and dendritic cells towards epithelial cells. C-terminal processed forms have been shown to be equally chemotactically active for leukocytes. CCL-20 holdes antibacterial activity e.coli atcc 25922 and s.aureus atcc 29213. CCL-20 gene transcription is activated by H. pylori, which activates NF-kappaB through intracellular signal pathway which involves IkappaB kinase and NF-kappaB-inducing kinase. MIP-3 alpha is invloved in chemokine-mediated lymphocyte trafficking during gastric inflammation in Helicobacter infection. CCL-20 expression is involved in the recruitment of CD45R0-positive T cell subsets into the intestinal lamina propria. MIP-3A is in charge of the advancement of pulpal inflammation through the recruitment of C-C motif Receptor 6-expressing lymphocytes Vaginal epithelial cells respond to factors present in semen by secreting MIP-3 alpha, which increases langerhans cells recruitment during HIV transmission.
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Synonyms
S Small inducible cytokine A20 precursor, CCL20, Macrophage inflammatory protein 3 alpha, MIP-3-alpha, Liver and activation- regulated chemokine, CC chemokine LARC, Beta chemokine exodus-1, CKb4, LARC, ST38, MIP3A, MIP-3a, SCYA20.
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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 MASNFDCCLG YTDRILHPKF IVGFTRQLAN EGCDINAIIF HTKKKLSVCA NPKQTWVKYI VRLLSKKVKN M.
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Background
What is the molecular weight/Mw of CCL20 HUMAN, HIS Protein?
CCL20 HUMAN, HIS Protein has a total Mw of 10.3kDa.
What is the source or expression system of CCL20 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CCL20 HUMAN, HIS Protein?
CCL20 HUMAN, HIS Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL20 HUMAN, HIS Protein?
The biological functionality of CCL20 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CCL20 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MASNFDCCLG YTDRILHPKF IVGFTRQLAN EGCDINAIIF HTKKKLSVCA NPKQTWVKYI VRLLSKKVKN M.
What applications can CCL20 HUMAN, HIS Protein be used in?
CCL20 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL20 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL20 HUMAN, 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.
- View Data Sheet
Name :
OSM Human, 209 a.aDescription:
Oncostatin M Human Recombinant (209 a.a.)
OSM, MGC20461, Oncostatin M.
Product # :
CYT-639Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Oncostatin-M (209 a.a.) Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 209 amino acids and having a molecular mass of 23.9kDa. The Oncostatin-M (209 a.a.) is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Oncostatin-M (209 a.a.) was lyophilized from a concentrated (1mg/ml) solution containing 1x PBS pH-7.4.
Purity
Greater than 97.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of Human TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000 IU/mg.More Info
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Introduction
Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.
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Synonyms
OSM, MGC20461, Oncostatin M.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Oncostatin-M (209 a.a.) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin-M (209 a.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 Oncostatin-M (209 a.a.) 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
AAIGSCSKEYRVLLGQLQKQTDLMQDTSRLLDPYIRIQGLDVPKLREHCRERPG
AFPSEETLRGLGRRGFLQTLNATLGCVLHRLADLEQRLPKAQDLERSGLNIEDL
EKLQMARPNILGLRNNIYCMAQLLDNSDTAEPTKAGRGASQPPTPTPASDAFQ
RKLEGCRFLHGYHRFMHSVGRVFKWGESPNRSRRHSPHQALRKGVRR.
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 :
Lymphotactin Human, HisDescription:
Lymphotactin Human Recombinant (XCL1), His Tag
XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.
Product # :
CHM-357Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
XCL1 Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 114 amino acids (22-114 a.a.) and having a molecular mass of 12.5 kDa. The XCL1 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Recombinant XCL1 contains 20mM Tris buffer pH-8, 200mM NaCl, 2mM DTT and 30% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
XCL1 is a small cytokine belonging to the XC chemokine family that is also known as lymphotactin. It is located in high levels in spleen, thymus, intestine and peripheral blood leukocytes, and at lower levels in lung, prostate gland and ovary. Cellular sources for XCL1 include activated thymic and peripheral blood CD8+ T cells. This chemokine attracts T cells. In humans, XCL1 is closely related to another chemokine called XCL2, whose gene is found at the same locus on chromosome 1. XCL1 induces it chemotactic function by binding to a chemokine receptor called XCR1.
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Synonyms
XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.
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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 MVGSEVSDKR TCVSLTTQRL PVSRIKTYTI TEGSLRAVIF ITKRGLKVCA DPQATWVRDV VRSMDRKSNT RNNMIQTKPT GTQQSTNTAV TLTG.
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 :
DNAJC15 HumanDescription:
DnaJ (Hsp40) Homolog, Subfamily C, Member 15 Human Recombinant
DnaJ homolog subfamily C member 15, Cell growth-inhibiting gene 22 protein, Methylation-controlled J protein, MCJ, DNAJC15, DNAJD1, GIG22, HSD18.
Product # :
HSP-057Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
DNAJC15 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 116 amino acids (58-150 a.a.) and having a molecular mass of 12.8 kDa.DNAJC15 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The DNAJC15 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
DNAJC15 which is expressed ubiquitously and located on the membrane contains 1 J domain. In many advanced cases of ovarian adenocarcinoma DNAJC15 is absent or down-regulated, due to hypermethylation and allelic loss. Loss of expression correlates with increased resistance to antineoplastic drugs, such as cisplatin. DNAJC15is a crucial component of the TIM23 translocase complex and stimulates the ATPase activity of HSPA9.
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Synonyms
DnaJ homolog subfamily C member 15, Cell growth-inhibiting gene 22 protein, Methylation-controlled J protein, MCJ, DNAJC15, DNAJD1, GIG22, HSD18.
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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 MGSFRIWKPL EQVITETAKK ISTPSFSSYY KGGFEQKMSR REAGLILGVS PSAGKAKIRT AHRRVMILNH PDKGGSPYVA AKINEAKDLL ETTTKH.
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.