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1000 results found for “Cyclophilin”
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Name :
PFN2 HumanDescription:
Profilin-2 Human Recombinant
Profilin-II, PFN2, Profilin-2, PFL, D3S1319E.
Product # :
PRO-809Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PFN2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids (1-140 a.a.) and having a molecular mass of 17.2 kDa. PFN2 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
PFN2 protein solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
PFN2 is a ubiquitous actin monomer-binding protein which is part of the profilin family. PFN2 regulates actin polymerization in response to extra cellular signals. PFN2 binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, while it increases it at low concentrations. PFN2 binds to PIP2, it inhibits the formation of IP3 and DG.
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Synonyms
Profilin-II, PFN2, Profilin-2, PFL, D3S1319E.
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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 MAGWQSYVDN LMCDGCCQEA AIVGYCDAKY VWAATAGGVF QSITPIEIDM IVGKDREGFF TNGLALGAKK CSVIRDSLYV DGDCTMDIRT KSQGGEPTYN VAVGRAGRVL VFVMGKEGVH GGGLNKKAYS MAKYLRDSGF.
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 :
RCVRN MouseDescription:
Recoverin Mouse Recombinant
RCV1, Cancer-associated retinopathy protein, Protein CAR, RCVRN, Recoverin, S-modulin.
Product # :
PRO-2547Price :
Quantity :
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Shipped with Ice Packs
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Description
Recoverin Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (1-202a.a.) and having a molecular mass of 25.8kDa. Recoverin Mouse is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) contains Phosphate Buffered Saline (pH 7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% 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, S-modulin.
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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 MGSMGNSKSG ALSKEILEEL QLNTKFTEEE LSAWYQSFLK ECPSGRITRQ EFESIYSKFF PDSDPKAYAQ HVFRSFDANS DGTLDFKEYV IALHMTTAGK PTQKLEWAFS LYDVDGNGTI SKNEVLEIVM AIFKMIKPED VKLLPDDENT PEKRAEKIWA FFGKKEDDKL TEEEFIEGTL ANKEILRLIQ FEPQKVKERI KEKKQ.
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 :
CRYGD MouseDescription:
Crystallin, Gamma D Mouse Recombinant
Gamma-crystallin D, Gamma-D-crystallin , Gamma-crystallin 1, CRYGD.
Product # :
PRO-2484Price :
Quantity :
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Description
CRYGD Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (1-174 a.a.) and having a molecular mass of 23.5kDa.CRYGD is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CRYGD protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CRYGD is a member of the beta/gamma-crystallin family. Crystallins are the principal structural components of the vertebrate eye lens. The mammalian lens crystallins are divided into alpha, beta, and gamma families. Gamma-crystallins are involved in cataract formation. Defects in the CRYGD gene are responsible for cataract autosomal dominant (ADC), cataract congenital non-nuclear polymorphic autosomal dominant (CCP), cataract congenital cerulean type 3 (CCA3) and cataract crystalline aculeiform (CACA).
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Synonyms
Gamma-crystallin D, Gamma-D-crystallin , Gamma-crystallin 1, CRYGD.
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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 MGSMGKITFY EDRGFQGRHY ECSTDHSNLQ PYFSRCNSVR VDSGCWMLYE QPNFTGCQYF LRRGDYPDYQ QWMGFSDSVR SCRLIPHAGS HRIRLYEREE YRGQMIEFTE DCPSLQDRFH FNEIYSLNVL EGCWVLYDMT NYRGRQYLLR PGEYRRYHDW
GAMNARVGSL RRVMDFY
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 :
CST11 HumanDescription:
Cystatin 11 Human Recombinant
CST8L, CTES2, dJ322G13.6, SC13.
Product # :
PRO-1475Price :
Quantity :
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Shipped with Ice Packs
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Description
CST11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (26-103 a.a.) and having a molecular mass of 11.8kDa.CST11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CST11 protein 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
Cystatin 11 (CST11) is a member of the Cystatin family. The Cystatin superfamily is comprised of proteins with multiple cystatin-like sequences. Several family members are active cysteine protease inhibitors, other family members have lost or perhaps never developed this inhibitory activity. The Cystatin superfamily consists of three inhibitory families, including the type 1 cystatins (stefins), type 2 cystatins and the kininogens. The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. The majority of the type 2 cystatin genes and pseudogenes are contained in the cystatin locus on chromosome 20. CST11 is located in the cystatin locus and encodes an epididymal-specific protein whose specific function has not been verified yet.
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Synonyms
CST8L, CTES2, dJ322G13.6, SC13.
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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 MGSARKKTFL SVHEVMAVEN YAKDSLQWIT DQYNKESDDK YHFRIFRVLK VQRQQVNCFF SVFAVPWFEQ YKILNKSCSS D.
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 :
CSTF1 HumanDescription:
Cleavage Stimulation Factor 1 Human Recombinant
Cleavage stimulation factor subunit 1, CF-1 50 kDa subunit, Cleavage stimulation factor 50 kDa subunit, CSTF 50 kDa subunit, CstF-50, CSTF1, CstFp50.
Product # :
PRO-1170Price :
Quantity :
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Shipped with Ice Packs
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Description
CSTF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 439 amino acids (1-431 a.a) and having a molecular mass of 49.4kDa.CSTF1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CSTF1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2M urea.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Cleavage stimulation factor subunit 1 (CSTF1) is involved in the polyadenylation and 3'end cleavage of pre-mRNAs. The CSTF1 gene encodes one of three subunits which merge to produce cleavage stimulation factor (CSTF). Like the mammalian G protein beta subunits, CSTF1 contains transducin-like repeats. CSTF1 is one of the numerous factors necessary for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. CSTF1 is responsible for the interaction of CSTF with other factors to create a stable complex on the pre-mRNA.
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Synonyms
Cleavage stimulation factor subunit 1, CF-1 50 kDa subunit, Cleavage stimulation factor 50 kDa subunit, CSTF 50 kDa subunit, CstF-50, CSTF1, CstFp50.
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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
MYRTKVGLKD RQQLYKLIIS QLLYDGYISI ANGLINEIKP QSVCAPSEQL LHLIKLGMEN DDTAVQYAIG RSDTVAPGTG IDLEFDADVQ TMSPEASEYE TCYVTSHKGP CRVATYSRDG QLIATGSADA SIKILDTERM LAKSAMPIEV MMNETAQQNM ENHPVIRTLY DHVDEVTCLA FHPTEQILAS GSRDYTLKLF DYSKPSAKRA FKYIQEAEML RSISFHPSGD FILVGTQHPT LRLYDINTFQ CFVSCNPQDQ HTDAICSVNY NSSANMYVTG SKDGCIKLWD GVSNRCITTF EKAHDGAEVC SAIFSKNSKY ILSSGKDSVA KLWEISTGRT LVRYTGAGLS GRQVHRTQAV FNHTEDYVLL PDERTISLCC WDSRTAERRN LLSLGHNNIV RCIVHSPTNP GFMTCSDDFR ARFWYRRSTT DVEHHHHHH.
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 :
EMAP II HumanDescription:
Endothelial-Monocyte Activating Polypeptide II Human Recombinant
AIMP1, EMAP2, EMAP-2, EMAPII, SCYE1, Multisynthetase complex auxiliary component p43, Endothelial monocyte-activating polypeptide 2, EMAP-II, p43.
Product # :
CYT-607Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
EMAP-II Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 166 amino acids and having a molecular mass of 18.3 kDa. The EMAP-II is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM sodium Phosphate buffer pH=7.5 and 130mM sodium chloride.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by the apoptotic effect on MCF-7 cells using a concentration of 20-30 ng/ml.More Info
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Introduction
EMAP-II also called SCYE1 is a tumor derived cytokine that plays a role in a wide variety of activities on endothelial cells, monocytes and neutrophils. EMAP-II inhibits endothelial cell proliferation, vasculogenesis, neovessel formation, and can induce apoptosis. It is also chemotactic towards neutrophils and monocytes and induces myeloperoxidase activity from neutrophils. EMAP-II clinical value is inhibiting angiogenesis of vascular beds and suppressing the growth of primary and secondary tumors with no affect to normal tissues. SCYE1is specifically induced by apoptosis, and it is involved in the control of angiogenesis, inflammation, and wound healing. The release of this SCYE1 renders the tumor-associated vasculature sensitive to tumor necrosis factor. The precursor protein is identical to the p43 subunit, which is associated with the multi-tRNA synthetase complex, and it modulates aminoacylation activity of tRNA synthetase in normal cells. EMAP-2 plays a role in in the stimulation of inflammatory responses after proteolytic cleavage in tumor cells.
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Synonyms
AIMP1, EMAP2, EMAP-2, EMAPII, SCYE1, Multisynthetase complex auxiliary component p43, Endothelial monocyte-activating polypeptide 2, EMAP-II, p43.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized EMAP-II although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EMAP-II 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 EMAP-II 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
SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQM QNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.
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Background
What is the molecular weight/Mw of EMAP II HUMAN Protein?
EMAP II HUMAN Protein has a total Mw of 18.3kDa.
What is the source or expression system of EMAP II HUMAN Protein?
Escherichia Coli.
What is the Purity of EMAP II HUMAN Protein?
EMAP II HUMAN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of EMAP II HUMAN Protein?
Determined by the apoptotic effect on MCF-7 cells using a concentration of 20-30 ng/ml.
What is the amino acid sequence of EMAP II HUMAN Protein?
SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQM QNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.
What applications can EMAP II HUMAN Protein be used in?
EMAP II HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EMAP II HUMAN Protein?
The endotoxin level is minimal, EMAP II 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 :
TFF1 HumanDescription:
Trefoil Factor-1 Human Recombinant
TFF-1, TFF1, pS2, BCEI, HPS, HP1.A, pNR-2, D21S21, pS2 protein, Trefoil factor 1, Breast cancer estrogen-inducible protein.
Product # :
CYT-586Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TFF-1 Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 60 amino acids which includes a 40 amino acid trefoil motif containing 3 conserved intramolecular disulfide bonds and having a total molecular mass of 13.2 kDa. TFF-1 Human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Human TFF1 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.4 and 150mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a chemotaxis bioassay using human MCF-7 cells is less than 10µg/ml, corresponding to a specific activity of >100 IU/mg.More Info
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Introduction
The Trefoil Factor peptides (TFF1, TFF2 and TFF3) are stable secretory proteins expressed in the gastrointestinal tract (gastric mucosa), and are involved in intestinal mucosal defense and repair. TFF1 is an essential protein for normal differentiation of the antral and pyloric gastric mucosa and functions as a gastric-specific tumor suppressor gene. TFF1 is a stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. TFF1 protects the mucosa from isults, stabilizes the mucus layer, & affects healing of the epithelium. TFF1 is commonly expressed in tumors. TFF1 is related with the cell membrane of MCF-7 cells. High levels of TFF1 and TFF2 are found in serum from inflammatory bowel disease.
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Synonyms
TFF-1, TFF1, pS2, BCEI, HPS, HP1.A, pNR-2, D21S21, pS2 protein, Trefoil factor 1, Breast cancer estrogen-inducible protein.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TFF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF1 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 TFF1 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
EAQTETCTVAPRERQNCGFPGVTPSQCANKGCCFDDTVRGVPWCFY
PNTIDVPPEEECEF.
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 :
CAPSL HumanDescription:
Calcyphosine-Like Human Recombinant
Calcyphosine-like protein, CAPSL, MGC26610.
Product # :
PRO-185Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CAPSL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 228 amino acids (1-208) and having a molecular mass of 26.3 kDa.The CAPSL is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CAPSL protein at 1mg/ml in 20mM Tris-HCL, pH-8, 0.2M NaCl, 5mM DTT and 20% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CAPSL is a calcium-binding protein holding two conserved calcium-binding motifs (EF-hands) which are found in a superfamily of calcium sensors and calcium signal modulators. In addition, the CAPSL gene is in the same linkage disequilibrium (LD) block as the IL7R gene and there is well known association between the CAPSL-IL7R locus and type 1 diabetes.
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Synonyms
Calcyphosine-like protein, CAPSL, MGC26610.
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Physical Appearance
CAPSL 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 MAGTARHDRE MAIQAKKKLT TATDPIERLR LQCLARGSAG IKGLGRVFRI MDDDNNRTLD FKEFMKGLND YAVVMEKEEV EELFQRFDKD GNGTIDFNEF LLTLRPPMSR ARKEVIMQAF RKLDKTGDGV ITIEDLREVY NAKHHPKYQN GEWSEEQVFR KFLDNFDSPY DKDGLVTPEE FMNYYAGVSA SIDTDVYFII MMRTAWKL
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 :
NRP1 HumanDescription:
Neuropilin 1 Human Recombinant
Neuropilin-1 isoform a, NRP1, BDCA4, CD304, NP1, NRP, VEGF165R, Vascular endothelial cell growth factor 165 receptor.
Product # :
CYT-1059Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NRP1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 843 amino acids (22-856a.a.) and having a molecular mass of 94.8kDa. (Molecular size on SDS-PAGE will appear at approximately 100-150kDa).NRP1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
NRP1 protein solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
NRP1 is a coreceptor bound on membranes to tyrosine kinase receptors for semaphorin family proteins and endothelial growth factors, it is a type one transmembrane protein. Neuropilin-1 takes part in cell survival, angiogenesis, invasion, migration, and axon guidance. the protein is a potential target for cancer therapies as it interacts with VEGF (co-receptor).
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Synonyms
Neuropilin-1 isoform a, NRP1, BDCA4, CD304, NP1, NRP, VEGF165R, Vascular endothelial cell growth factor 165 receptor.
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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
FRNDKCGDTI KIESPGYLTS PGYPHSYHPS EKCEWLIQAP DPYQRIMINF NPHFDLEDRD CKYDYVEVFD GENENGHFRG KFCGKIAPPP VVSSGPFLFI KFVSDYETHG AGFSIRYEIF KRGPECSQNY TTPSGVIKSP GFPEKYPNSL ECTYIVFAPK MSEIILEFES FDLEPDSNPP
GGMFCRYDRL EIWDGFPDVG PHIGRYCGQK TPGRIRSSSG ILSMVFYTDS AIAKEGFSAN YSVLQSSVSE DFKCMEALGM ESGEIHSDQI TASSQYSTNW SAERSRLNYP ENGWTPGEDS YREWIQVDLG LLRFVTAVGT QGAISKETKK KYYVKTYKID VSSNGEDWIT IKEGNKPVLF
QGNTNPTDVV VAVFPKPLIT RFVRIKPATW ETGISMRFEV YGCKITDYPC SGMLGMVSGL ISDSQITSSN QGDRNWMPEN IRLVTSRSGW ALPPAPHSYI NEWLQIDLGE EKIVRGIIIQ GGKHRENKVF MRKFKIGYSN NGSDWKMIMD DSKRKAKSFE GNNNYDTPEL RTFPALSTRF
IRIYPERATH GGLGLRMELL GCEVEAPTAG PTTPNGNLVD ECDDDQANCH SGTGDDFQLT GGTTVLATEK PTVIDSTIQS EFPTYGFNCE FGWGSHKTFC HWEHDNHVQL KWSVLTSKTG PIQDHTGDGN FIYSQADENQ KGKVARLVSP VVYSQNSAHC MTFWYHMSGS HVGTLRVKLR
YQKPEEYDQL VWMAIGHQGD HWKEGRVLLH KSLKLYQVIF EGEIGKGNLG GIAVDDISIN NHISQEDCAK PADLDKKNPE IKIDETGSTP GYEGEGEGDK NISRKPGNVL KTLDPLEHHH HHH.
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 :
STMN2 HumanDescription:
Stathmin Like-2 Human Recombinant
SCG10, STMB2, SCGN10, AI159727, STMN-2, Stathmin-2, Superior cervical ganglion-10 protein, Protein SCG10, STMN2, SGC10, stathmin-like 2.
Product # :
PRO-752Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human Stathmin Like-2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 142 amino acids (39-179 a.a) and having a molecular mass of 16.4 kDa. STMN2 is purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The STMN2 protein solution contains 50mM MES, pH-6.0, 0.1mM PMSF, 1 mM EDTA and 10% Glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
STMN2 is a neuronal growth-associated protein which shares a majority of its amino acid sequence with the phosphoprotein stathmin. STMN2 is involved in neuronal differentiation and in modulating membrane interaction with the cytoskeleton through neurite outgrowth. STMN2 is necessary for maintaining the anchorage-independent growth state of beta-catenin/TCF-activated hepatoma cells. SCG10 is a novel indicator of osteogenesis and osteoblast that takes part in the regulation of the adipocyte/osteoblast balance. STMN2 plays a role as an effector downstream of Rnd1 to regulate axon extensions by modulating microtubule organization.
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Synonyms
SCG10, STMB2, SCGN10, AI159727, STMN-2, Stathmin-2, Superior cervical ganglion-10 protein, Protein SCG10, STMN2, SGC10, stathmin-like 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
MDMEVKQINK RASGQAFELI LKPPSPISEA PRTLASPKKK DLSLEEIQKK LEAAEERRKS QEAQVLKQLA EKREHEREVL QKALEENNNF SKMAEEKLIL KMEQIKENRE ANLAAIIERL QEKERHAAEV RRNKELQVEL SG.
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 :
CGREF1 HumanDescription:
Cell Growth Regulator With EF-Hand Domain 1 Human Recombinant
Cell Growth Regulator With EF-Hand Domain 1, Cell Growth Regulatory Gene 11 Protein, Hydrophobestin, CGR11, Cell Growth Regulator With EF Hand Domain Protein 1, Cell Growth Regulator With EF Hand Domain 1, Cell growth regulator with EF hand domain protein 1.
Product # :
PRO-2154Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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Description
CGREF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 305 amino acids (20-301 a.a) and having a molecular mass of 32.3kDa. CGREF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CGREF1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH7.4).
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
Cell Growth Regulator with EF-Hand Domain 1, also known as CGREF1 is a secreted calcium ion binding protein. CGREF1 includes two EF-hand domains & both EF-hands are essential for function. CGREF1 is most likely digested extracellularly by an unfamiliar serine protease generating extremely hydrophobic bioactive peptides. CGREF1 mediates cell-cell adhesion in a calcium-dependent manner. In addition, CGREF1 is capable to inhibit growth in more than a few cell lines.
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Synonyms
Cell Growth Regulator With EF-Hand Domain 1, Cell Growth Regulatory Gene 11 Protein, Hydrophobestin, CGR11, Cell Growth Regulator With EF Hand Domain Protein 1, Cell Growth Regulator With EF Hand Domain 1, Cell growth regulator with EF hand domain protein 1.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSAPKDGVT RPDSEVQHQL LPNPFQPGQE QLGLLQSYLK GLGRTEVQLE HLSREQVLLY LFALHDYDQS GQLDGLELLS MLTAALAPGA ANSPTTNPVI LIVDKVLETQ DLNGDGLMTP AELINFPGVA LRHVEPGEPL APSPQEPQAV GRQSLLAKSP LRQETQEAPG PREEAKGQVE ARRESLDPVQ EPGGQAEADG DVPGPRGEAE GQAEAKGDAP GPRGEAGGQA EAEGDAPGPR GEAGGQAEAR ENGEEAKELP GETLESKNTQ NDFEVHIVQV ENDEI.
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 :
NAIF1 HumanDescription:
Nuclear Apoptosis Inducing Factor 1 Human Recombinant
bA379C10.2, C9orf90, RP11-379C10.2, Nuclear apoptosis-inducing factor 1, NAIF1.
Product # :
PRO-1978Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
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Description
NAIF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (1-327 a.a) and having a molecular mass of 37.6kDa. NAIF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NAIF1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Nuclear Apoptosis Inducing Factor 1 (NAIF1) is a part of the NAIF1 family. NAIF1 Interacts with HARBI1 and Induces apoptosis.
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Synonyms
bA379C10.2, C9orf90, RP11-379C10.2, Nuclear apoptosis-inducing factor 1, NAIF1.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAVPAKK RKMNFSEREV EIIVEELELK KHLLVNHFNA GVPLAAKSAA WHGILRRVNA VATCRRELPE VKKKWSDLKT EVRRKVAQVR AAVEGGEAPG PTEEDGAGGP GTGGGSGGGG PAVAPVLLTP MQQRICNLLG EATIISLPST TEIHPVALGP SATAAAATVT LTQIPTETTY HTLEEGVVEY CTAEAPPPLP PETPVDMMAQ HADTSVKPQA LKSRIALNSA KLIQEQRVTN LHVKEIAQHL EQQNDLLQMI RRSQEVQACA QERQAQAMEG TQAALSVLIQ VLRPMIKDFR RYLQSNTANP APASDPGQVA QNGQPDSIIQ.
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 :
MYOZ1 HumanDescription:
Myozenin 1 Human Recombinant
CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.
Product # :
PRO-1652Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
MYOZ1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299 a.a.) and having a molecular mass of 34.1kDa.MYOZ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MYOZ1 protein 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
-
Introduction
Myozenin 1 (MYOZ1) is a member of the myozenin family. MYOZ1 is mostly expressed in the skeletal muscle. Members of the myozenin family act as calcineurin-interacting proteins which helps tether calcineurin to the sarcomere of cardiac and skeletal muscle. The myozenin family plays a significant role in modulation of calcineurin signaling.
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Synonyms
CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPLSGTP APNKKRKSSK LIMELTGGGQ ESSGLNLGKK ISVPRDVMLE ELSLLTNRGS KMFKLRQMRV EKFIYENHPD VFSDSSMDHF QKFLPTVGGQ LGTAGQGFSY SKSNGRGGSQ AGGSGSAGQY GSDQQHHLGS GSGAGGTGGP AGQAGRGGAA GTAGVGETGS GDQAGGEGKH ITVFKTYISP WERAMGVDPQ QKMELGIDLL AYGAKAELPK YKSFNRTAMP YGGYEKASKR MTFQMPKFDL GPLLSEPLVL YNQNLSNRPS FNRTPIPWLS SGEPVDYNVD IGIPLDGETE EL.
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 :
CXCL5 HumanDescription:
Epithelial Neutrophil-Activating Protein 78 Human Recombinant (CXCL5)
Small inducible cytokine B5, CXCL5, Epithelial-derived neutrophil-activating protein 78, Neutrophil-activating peptide ENA-78, ENA-78(1-78), chemokine (C-X-C motif) ligand 5, SCYB5.
Product # :
CHM-331Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Epithelial Neutrophil-Activating Protein 78 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 74 amino acids and having a molecular mass of 8020 Dalton. The CXCL5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CXCL5 was lyophilized from a concentrated (1mg/ml) solution in water containing no additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity was determined by measuring the dose dependent mobilization of intracellular calcium (calcium flux) with human neutrophils. Significant calcium mobilization is observed with 100ng/mL (corresponding to a Specific Activity of 10,000IU/mg) of recombinant human ENA-78.More Info
-
Introduction
Chemokine (C-X-C motif) ligand 5 (CXCL5) is a small cytokine belonging to the CXC chemokine family that is also known as epithelial-derived neutrophil-activating peptide 78 (ENA-78). It is produced following stimulation of cells with the inflammatory cytokines interleukin-1 or tumor necrosis factor-alpha. Expression of CXCL5 has also been observed in eosinophils, and can be inhibited with the type II IFN. This chemokine stimulates the chemotaxis of neutrophils possesses angiogenic properties. It elicits these effects by interacting with the cell surface chemokine receptor CXCR2. The gene for CXCL5 is encoded on four exons and is located on human chromosome 4 amongst several other CXC chemokine genes. CXCL5 has been implicated in connective tissue remodelling.
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Synonyms
Small inducible cytokine B5, CXCL5, Epithelial-derived neutrophil-activating protein 78, Neutrophil-activating peptide ENA-78, ENA-78(1-78), chemokine (C-X-C motif) ligand 5, SCYB5.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized ENA78 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL5 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 ENA-78 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
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala- Ala -Val-Leu-Arg.
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Background
What is the molecular weight/Mw of CXCL5 HUMAN Protein?
CXCL5 HUMAN Protein has a total Mw of 8.02kDa.
What is the source or expression system of CXCL5 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL5 HUMAN Protein?
CXCL5 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL5 HUMAN Protein?
The biological activity was determined by measuring the dose dependent mobilization of intracellular calcium (calcium flux) with human neutrophils. Significant calcium mobilization is observed with 100ng/mL (corresponding to a Specific Activity of 10,000IU/mg) of recombinant human ENA-78.
What is the amino acid sequence of CXCL5 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala- Ala -Val-Leu-Arg.
What applications can CXCL5 HUMAN Protein be used in?
CXCL5 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL5 HUMAN Protein?
The endotoxin level is minimal, CXCL5 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.
- View Data Sheet
Name :
CXCL5 MouseDescription:
Epithelial Neutrophil-Activating Protein 78 Mouse Recombinant (CXCL5)
C-X-C motif chemokine 5, Small-inducible cytokine B5, Cytokine LIX, Cxcl5, Scyb5, LIX, GCP-2, Scyb6, ENA-78, AMCF-II.
Product # :
CHM-365Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
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- purity
- biological activity
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Description
Epithelial Neutrophil-Activating Protein 78 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 93 amino acids and having a molecular mass of 9.8kDa. The CXCL5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 20mM sodium phosphate buffer, pH 7.4 & 150mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.More Info
-
Introduction
Chemokine (C-X-C motif) ligand 5 (CXCL5) is a small cytokine belonging to the CXC chemokine family that is also known as epithelial-derived neutrophil-activating peptide 78 (ENA-78). It is produced following stimulation of cells with the inflammatory cytokines interleukin-1 or tumor necrosis factor-alpha. Expression of CXCL5 has also been observed in eosinophils. This chemokine stimulates the chemotaxis of neutrophils possesses angiogenic properties. It elicits these effects by interacting with the cell surface chemokine receptor CXCR2. The gene for CXCL5 is encoded on four exons and is located on human chromosome 4 amongst several other CXC chemokine genes. CXCL5 has been implicated in connective tissue remodelling.
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Synonyms
C-X-C motif chemokine 5, Small-inducible cytokine B5, Cytokine LIX, Cxcl5, Scyb5, LIX, GCP-2, Scyb6, ENA-78, AMCF-II.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized ENA-78 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL5 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized ENA-78 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
APSSVIAATE LRCVCLTVTP KINPKLIANL EVIPAGPQCP TVEVIAKLKN QKEVCLDPEA PVIKKIIIQK ILGSDKKKAK RNALAVERTA SVQ.
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Background
What is the molecular weight/Mw of CXCL5 MOUSE Protein?
CXCL5 MOUSE Protein has a total Mw of 9.8kDa.
What is the source or expression system of CXCL5 MOUSE Protein?
Escherichia Coli.
What is the Purity of CXCL5 MOUSE Protein?
CXCL5 MOUSE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL5 MOUSE Protein?
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.
What is the amino acid sequence of CXCL5 MOUSE Protein?
APSSVIAATE LRCVCLTVTP KINPKLIANL EVIPAGPQCP TVEVIAKLKN QKEVCLDPEA PVIKKIIIQK ILGSDKKKAK RNALAVERTA SVQ.
What applications can CXCL5 MOUSE Protein be used in?
CXCL5 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL5 MOUSE Protein?
The endotoxin level is minimal, CXCL5 MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Eotaxin HumanDescription:
Eotaxin Human Recombinant (CCL11)
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.
Product # :
CHM-256Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Eotaxin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 74 amino acids and having a molecular mass of 8345.9 Dalton. The CCL11 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 150mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is determined by the chemoattract of human PBE (peripheral blood eosinophils) at a concentration between 0.1-10 ng/ml corresponding to a Specific Activity of 100,000-10,000,000IU/mg.More Info
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Introduction
Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.
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Synonyms
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Eotaxin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL11 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 Eotaxin Human Recombinant 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
GPASVPTTCC FNLANRKIPL QRLESYRRIT SGKCPQKAVI FKTKLAKDICADPKKKWVQD
SMKYLDQKSP TPKP.
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Background
What is the molecular weight/Mw of EOTAXIN HUMAN Protein?
EOTAXIN HUMAN Protein has a total Mw of 8.3459kDa.
What is the source or expression system of EOTAXIN HUMAN Protein?
Escherichia Coli.
What is the Purity of EOTAXIN HUMAN Protein?
EOTAXIN HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of EOTAXIN HUMAN Protein?
The activity is determined by the chemoattract of human PBE (peripheral blood eosinophils) at a concentration between 0.1-10 ng/ml corresponding to a Specific Activity of 100,000-10,000,000IU/mg.
What is the amino acid sequence of EOTAXIN HUMAN Protein?
GPASVPTTCC FNLANRKIPL QRLESYRRIT SGKCPQKAVI FKTKLAKDICADPKKKWVQD
SMKYLDQKSP TPKP.
What applications can EOTAXIN HUMAN Protein be used in?
EOTAXIN HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EOTAXIN HUMAN Protein?
The endotoxin level is minimal, EOTAXIN 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.
- View Data Sheet
Name :
CX3CL1 HumanDescription:
Fractalkine Human Recombinant (CX3CL1)
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
Product # :
CHM-235Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
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- More Info
Description
Fractalkine Human Recombinant- produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 76 amino acids and having a molecular mass of 8638 Dalton. The Fractalkine is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CX3CL1 was lyophilized from a 0.2μm filtered concentrated (1.0 mg/ml) solution in 20mM Phosphate buffer, pH 7.4, 50mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Biological activity is calculated by its ability to chemoattract human T-Lymphocytes using a concentration range of 5.0-10.0 ng/ml corresponding to a Specific Activity of 100,000-200,000IU/mg.More Info
-
Introduction
Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.
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Synonyms
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized CX3CL1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CX3CL1 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 CX3CL1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
QHHGVTKCNITCSKMTSKIPVALLIHYQQNQASCGKRAIILETRQHRLFCADPKEQW VKDAMQHLDRQAAALTRNG.
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Background
What is the molecular weight/Mw of CX3CL1 HUMAN Protein?
CX3CL1 HUMAN Protein has a total Mw of 8.63kDa.
What is the source or expression system of CX3CL1 HUMAN Protein?
Escherichia Coli.
What is the Purity of CX3CL1 HUMAN Protein?
CX3CL1 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CX3CL1 HUMAN Protein?
The Biological activity is calculated by its ability to chemoattract human T-Lymphocytes using a concentration range of 5.0-10.0 ng/ml corresponding to a Specific Activity of 100,000-200,000IU/mg.
What is the amino acid sequence of CX3CL1 HUMAN Protein?
QHHGVTKCNITCSKMTSKIPVALLIHYQQNQASCGKRAIILETRQHRLFCADPKEQW VKDAMQHLDRQAAALTRNG.
What applications can CX3CL1 HUMAN Protein be used in?
CX3CL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CX3CL1 HUMAN Protein?
The endotoxin level is minimal, CX3CL1 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.
- View Data Sheet
Name :
VEGI HumanDescription:
Human Vascular Endothelial Growth Inhibitor Recombinant
Tumor necrosis factor ligand superfamily member 15, TNFSF-15, TNFSF15, TNF ligand-related molecule 1, VEGI, TL-1, TL1, TL1A, VEGI192A, VEGI-192, MGC129934, MGC129935.
Product # :
CYT-517Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
TNFSF15 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 20.5kDa. The TNFSF15 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TNFSF15 was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4 with 0.02% Tween-20.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by its ability to induce apoptosis using human TF-1 cells is less than 20ng/ml, corresponding to a specific activity of > 5.0×104 IU/mg.More Info
-
Introduction
TNFSF15 is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. This protein is abundantly expressed in endothelial cells, but is not expressed in either B or T cells. The expression of TNFSF15 is inducible by TNF and IL-1 alpha. This cytokine is a ligand for receptor TNFRSF25 and decoy receptor TNFRSF21/DR6. It can activate NF-kappaB and MAP kinases, and acts as an autocrine factor to induce apoptosis in endothelial cells. TNFSF15 is also found to inhibit endothelial cell proliferation, and thus may function as an angiogenesis inhibitor. An additional isoform encoded by an alternatively spliced transcript variant has been reported but the sequence of this transcript has not been determined.
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Synonyms
Tumor necrosis factor ligand superfamily member 15, TNFSF-15, TNFSF15, TNF ligand-related molecule 1, VEGI, TL-1, TL1, TL1A, VEGI192A, VEGI-192, MGC129934, MGC129935.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
TNFSF15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGI should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized TNFSF15 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MQLTKGRLHFSHPLSHTKHISPFVTDAPLRADGDKPRAHL
TVVRQTPTQHFKNQFPALHWEHELGLAFTKNRMNYTNKF
LLIPESGDYFIYSQVTFRGMTSECSEIRQAGRPNKPDSIT
VVITKVTDSYPEPTQLLMGTKSVCEVGSNWFQPIYLGAM
FSLQEGDKLMVNVSDISLVDYTKEDKTFFGAFLL.
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 :
CYTL1 HumanDescription:
Cytokine-Like 1 Human Recombinant
Cytokine-like protein 1, Protein C17, CYTL1, C4orf4, C17.
Product # :
CYT-775Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
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- purity
- More Info
Description
CYTL1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 23-136) containing 124 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 14.6kDa (calculated).
Source
Escherichia Coli.
Formulation
CYTL1 was filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Cytokine-like protein 1 (CYTL1) is a secreted protein. CYTL1 is expressed in CD34+ cell populations of bone marrow and cord blood which function as hematopoietic stem/progenitor cells. However, CYTL1 is not expressed in CD34- cells. Experiments with knock-out mice (Cytl1-/-) propose that CYTL1 is essential for the maintenance of cartilage homeostasis rather than cartilage and bone development, and loss of CYTL1 function is linked with experimental osteoarthritic cartilage destruction in mice.
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Synonyms
Cytokine-like protein 1, Protein C17, CYTL1, C4orf4, C17.
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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. CYTL1 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
MKHHHHHHASTPPTCYSRMR ALSQEITRDF NLLQVSEPSE PCVRYLPRLY LDIHNYCVLD KLRDFVASPP CWKVAQVDSL KDKARKLYTI MNSFCRRDLV FLLDDCNALE YPIPVTTVLP DRQR.
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Background
Title: Cytokine-Like 1 Human Recombinant: Exploring its Role in Immune Regulation and Therapeutic Potential
Abstract:
Cytokine-like 1 (CYTL1) is an emerging cytokine that exhibits pleiotropic effects on immune regulation and tissue homeostasis. This research paper provides a comprehensive analysis of human recombinant CYTL1, focusing on its production, characterization, and potential applications in immune modulation. The paper highlights the significance of CYTL1 in immune cell function, inflammation, and tissue repair. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant CYTL1 in various pathological conditions. The information presented in this paper aims to enhance our understanding of human recombinant CYTL1 and its utility as a research tool and a potential immunotherapeutic agent.Introduction:
Cytokine-like 1 (CYTL1) is a recently discovered cytokine with diverse biological functions, including immune regulation and tissue repair. Human recombinant CYTL1, produced through genetic engineering techniques, provides researchers with a valuable tool to study its biological activities and explore its therapeutic potential.Production and Characterization:
Recombinant CYTL1 is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CYTL1.Role in Immune Regulation:
CYTL1 has been shown to modulate immune cell function and inflammation. It can influence the differentiation and activation of various immune cell subsets, including T cells and macrophages. Recombinant CYTL1 serves as a valuable tool for investigating the mechanisms underlying immune regulation and exploring its potential as an immunomodulatory agent.Therapeutic Implications:
The dysregulation of immune responses is associated with numerous pathological conditions, including autoimmune diseases and chronic inflammation. Recombinant CYTL1 holds promise as a potential immunotherapeutic agent due to its ability to modulate immune cell function and regulate inflammatory processes. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant CYTL1 in various diseases, including autoimmune disorders and tissue regeneration.Conclusion:
Human recombinant CYTL1 is a valuable research tool and a potential immunotherapeutic agent. Its production, characterization, and applications in immune regulation contribute to our understanding of immune responses and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant CYTL1 offer promising avenues for improving outcomes in autoimmune diseases, chronic inflammation, and tissue repair.What is the molecular weight/Mw of CYTL1 Protein?
CYTL1 Protein has a total Mw of 14.6kDa.
What is the source or expression system of CYTL1 Protein?
Escherichia Coli.
What is the Purity of CYTL1 Protein?
CYTL1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CYTL1 Protein?
The biological functionality of CYTL1 Protein will be determined in the future.
What is the amino acid sequence of CYTL1 Protein?
MKHHHHHHASTPPTCYSRMR ALSQEITRDF NLLQVSEPSE PCVRYLPRLY LDIHNYCVLD KLRDFVASPP CWKVAQVDSL KDKARKLYTI MNSFCRRDLV FLLDDCNALE YPIPVTTVLP DRQR.
What applications can CYTL1 Protein be used in?
CYTL1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CYTL1 Protein?
The endotoxin level is minimal, CYTL1 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 :
CXCL4 Variant 1 HumanDescription:
Platelet Factor-4 Variant 1 Human Recombinant
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
Product # :
CHM-243Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
CXCL4 Variant-1 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. The CXCL4 Variant-1 is fused to 6xHis tag at N-Terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized without additives.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets . Its major physiologic role appears to be neutralization of molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemocinfamily. Human PF4 is used for the proof of induced thrombocytopenia. Furthermore it is used as an inhibitor in the angiogenesis during tumor therapy.
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Synonyms
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Human CXCL4 although stable at 25°C 1 week, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CXCL4 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
MHHHHHHEAE EDGDLQCLCV KTTSQVRPRH ITSLEVIKAG PHCPTAQLIA TLKNGRKICL DLQALLYKKI IKEHLES.
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 :
Cys-Protein-GDescription:
Cys-Protein G Recombinant
Product # :
PRO-1238Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- source
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Description
Cys-Protein G Recombinant produced in E.Coli, is a single non-glycosylated polypeptide chain containing 201 amino acids and having a cys on N-terminal. Cys-Protein G has a predicted molecular mass of approximately 21.9kDa but it migrates with an apparent molecular mass of 40kDa in SDS-PAGE. The Cys-Protein G is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized without any additives.
Purity
Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein G 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 Protein G in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
CLPKTDTYKL ILNGKTLKGE TTTEAVDAAT AEKVFKQYAN DNGVDGEWTY DDATKTFTVT EKPEVIDASE LTPAVTTYKL VINGKTLKGE TTTEAVDAAT AEKVFKQYAN DNGVDGEWTY DDATKTFTVT EKPEVIDASE LTPAVTTYKL VINGKTLKGE TTTKAVDAET AEKAFKQYAN DNGVDGVWTY DDATKTFTVT E.
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Specificity
The recombinant Protein G is a genetically engineered protein contains 3 IgG-binding regions of protein G.
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 :
CCDC101 HumanDescription:
Coiled-Coil Domain Containing 101 Human Recombinant
coiled-coil domain containing protein 101, SAGA-associated factor 29 homolog, SGF29, STAF36, FLJ32446.
Product # :
PRO-1063Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
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Description
CCDC101 Human Recombinant produced in E. coli is a single polypeptide chain containing 313 amino acids (1-293) and having a molecular mass of 35.4kDa.CCDC101 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CCDC101 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
CCDC101 is known as a subunit of the SAGA (Spt-Ada-Gcn5 acetyltransferase) histone acetyltransferase complex in Saccharomyces cerevisiae. CCDC101 is conserved from yeast to humans.
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Synonyms
coiled-coil domain containing protein 101, SAGA-associated factor 29 homolog, SGF29, STAF36, FLJ32446.
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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 MALVSADSRI AELLTELHQL IKQTQEERSR SEHNLVNIQK THERMQTENK ISPYYRTKLR GLYTTAKADA EAECNILRKA LDKIAEIKSL LEERRIAAKI AGLYNDSEPP RKTMRRGVLM TLLQQSAMTL PLWIGKPGDK PPPLCGAIPA SGDYVARPGD KVAARVKAVD GDEQWILAEV VSYSHATNKY EVDDIDEEGK ERHTLSRRRV IPLPQWKANP ETDPEALFQK EQLVLALYPQ TTCFYRALIH APPQRPQDDY SVLFEDTSYA DGYSPPLNVA QRYVVACKEP KKK
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 :
CRISP2 HumanDescription:
Cysteine-Rich Secretory Protein 2 Human Recombinant
Cysteine-Rich Secretory Protein 2, Cancer/Testis Antigen 36, TPX1, Testis Specific Protein 1 (Probe H4-1 P3-1), Testis-Specific Protein TPX-1, CRISP-2, GAPDL5, TSP1, CT36, Glyceraldehyde-3-Phosphate Dehydrogenase-Like 5, CRISP2.
Product # :
PRO-2030Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CRISP2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (22-243) containing 232 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 26.32kDa.
Source
Escherichia Coli.
Formulation
CRISP2 filtered (0.4µm) solution at a concentration of 0.3mg/ml in 50mM acetate buffer, pH 4, 5mM DTT and 20%glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cysteine-Rich Secretory Protein 2 (CRISP2) regulates some ion channels activity and thereby regulates calcium fluxes during sperm capacitation. Amongst its related pathways are p53 signaling. Diseases related with CRISP2 include epididymitis and orchitis.
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Synonyms
Cysteine-Rich Secretory Protein 2, Cancer/Testis Antigen 36, TPX1, Testis Specific Protein 1 (Probe H4-1 P3-1), Testis-Specific Protein TPX-1, CRISP-2, GAPDL5, TSP1, CT36, Glyceraldehyde-3-Phosphate Dehydrogenase-Like 5, CRISP2.
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Physical Appearance
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
MKHHHHHHASKDPAFTALLT TQLQVQREIV NKHNELRKAV SPPASNMLKM EWSREVTTNA QRWANKCTLQ HSDPEDRKTS TRCGENLYMS SDPTSWSSAI QSWYDEILDF VYGVGPKSPN AVVGHYTQLV WYSTYQVGCG IAYCPNQDSL KYYYVCQYCP AGNNMNRKNT PYQQGTPCAG CPDDCDKGLC TNSCQYQDLL SNCDSLKNTA GCEHELLKEK CKATCLCENK IY.
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 :
Resistin Human, HEKDescription:
Resistin Human Recombinant, HEK
RETN,ADSF,FIZZ3,RETN1,RSTN,XCP1,resistin precursor, Adipose tissue-specific secretory factor, ADSFMGC126609, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, Cysteine-rich secreted protein FIZZ3, FIZZ3; FIZZ3MGC126603, found in inflammatory zone 3, HXCP1.
Product # :
CYT-1183Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- source
- formulation
- purity
- More Info
Description
Resistin Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (19-108 a.a) containing 96 amino acids and having a molecular mass of 10.3 kDa.Resistin is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
Resistin protein (1mg/ml) contains 20% glycerol and 20mM Sodium citrate (pH3.0).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Resistin, also known as adipose tissue-specific secretory factor (ADSF) is a cysteine-rich peptide derived from adipose tissue. Resistin takes part in the inflammatory response, glucose metabolism, and angiogenesis.Resistin blocks insulinstimulated uptake of glucose by adipocytes and promote glucose release by hepatocytes. As such,Resistin considered to participate in diet‑induced insulin-sensitivity. Resistin causes high levels of lowdensity lipoprotein (LDL), increasing the risk of heart disease.
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Synonyms
RETN,ADSF,FIZZ3,RETN1,RSTN,XCP1,resistin precursor, Adipose tissue-specific secretory factor, ADSFMGC126609, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, Cysteine-rich secreted protein FIZZ3, FIZZ3; FIZZ3MGC126603, found in inflammatory zone 3, HXCP1.
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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
KTLCSMEEAI NERIQEVAGS LIFRAISSIG LECQSVTSRG DLATCPRGFA VTGCTCGSAC GSWDVRAETT CHCQCAGMDW TGARCCRVQP HHHHHH
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.