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1000 results found for “secretogranin”
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Name :
CST6 Human, ActiveDescription:
Cystatin E/M, BioActive Human Recombinant
Cystatin E/M, cystatin 6, Cystatin M, Cystatin-E, Cysteine proteinase inhibitor.
Product # :
PRO-2633Price :
Quantity :
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Shipped with Ice Packs
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Description
CST6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 142 amino acids (29-149 a.a.) and having a molecular mass of 15.9kDa.CST6 is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CST6 solution (0.5mg/1ml) contains 10% glycerol, 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The IC50 value is < 10nM. The inhibitory function of Cystatin 6 on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25˚C.
More Info
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Introduction
Cystatin E/M or CST6 is part of the cystatin type 2 family. Part of the cystatin type 2 family members can act as cysteine protease inhibitors, whereas cystatin E/M regulates cathepsin B inhibitors and not cathepsin C. cystatin E/M is a protein the when secreted, has an effect on osteogenesis and bone resorption, insulin regulation, response to systemic inflammation & hepatocyte growth factor receptors.
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Synonyms
Cystatin E/M, cystatin 6, Cystatin M, Cystatin-E, Cysteine proteinase inhibitor.
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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 MRPQERMVGE LRDLSPDDPQ VQKAAQAAVA SYNMGSNSIY YFRDTHIIKA QSQLVAGIKY FLTMEMGSTD CRKTRVTGDH VDLTTCPLAA GAQQEKLRCD FEVLVVPWQN SSQLLKHNCV QM
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 :
TGM2 HumanDescription:
Tissue Transglutaminase Human Recombinant
Protein gamma-glutamyltransferase 2, EC 2.3.2.13, Tissue transglutaminase, TGase C, TGC, TG(C), Transglutaminase-2, TGase-H, TG2, TGM2.
Product # :
ENZ-394Price :
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Shipped with Ice Packs
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Description
Tissue Transglutaminase Human Recombinant produced in E.coli is a non-glycosylated, polypeptide chain having a molecular mass of 78,018 Dalton. tTG is expressed with a -6xHis tag and purified by proprietary chromatographic techniques. By point mutation of the active center the catalytic transglutaminase activity has been eliminated, resulting in increased stability during storage and coating.
Source
Escherichia Coli.
Formulation
TGM2 is supplied in 16mM HEPES buffer pH-8.0, 400mM NaCl, and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Celiac disease is an enteropathy that is characterized by intestinal lesions of variable severity. Tissue-type transglutaminase (tTG) is believed to be the predominant autoantigen for celiac disease and the corresponding autoantibodies show higher sensitivity and specificity than anti-gliadin antibodies. Highly pure recombinant human tTG is now available to replace the traditionally used tTG fraction from guinea pig.
Tissue-type transglutaminase antigens have been specifically modified for improved handling: exchange of an active site amino acid eliminates the protein cross-linking activity of the enzyme, while maintaining the native three-dimensional structure and the enzyme's secondary GTPase activity. This engineering assures reproducible properties of the antigen preparations through the absence of variable and ill-defined covalent aggregates of tTG antigen and host cell proteins. -
Synonyms
Protein gamma-glutamyltransferase 2, EC 2.3.2.13, Tissue transglutaminase, TGase C, TGC, TG(C), Transglutaminase-2, TGase-H, TG2, TGM2.
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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. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
FGF 2 Human (147 a.a.)Description:
Fibroblast Growth Factor Basic 147 a.a. Human Recombinant
Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.
Product # :
CYT-557Price :
Quantity :
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Shipped at Room temp
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Description
Fibroblast Growth Factor-2 Human Recombinant (FGF-2) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 147 amino acids and having a molecular mass of 16.5kDa. The FGF2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The bFGF was lyophilized from a sterile filtered solution containing 20mM Tris-HCl, pH 7.6 and 150mM NaCl.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Biological Activity
The ED50, Calculated by the dose- dependent proliferation of mouse BALB/c 3T3 cells is < 0.05ng/ml corresponding to a specific activity of 2.0x107 units/mg.
More Info
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Introduction
FGF-basic is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.
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Synonyms
Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized basic-FGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGFb 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 FGF-B 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
MPALPEDGGS GAFPPGHFKD PKRLYCKNGG FFLRIHPDGR VDGVREKSDP HIKLQLQAEE RGVVSIKGVC ANRYLAMKED GRLLASKCVT DECFFFERLE SNNYNTYRSR KYTSWYVALK RTGQYKLGSK TGPGQKAILF LPMSAKS.
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Background
What is the molecular weight/Mw of FGF 2 Protein?
FGF 2 Protein has a total Mw of 16.5kDa.
What is the source or expression system of FGF 2 Protein?
Escherichia Coli.
What is the Purity of FGF 2 Protein?
FGF 2 Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF 2 Protein?
The ED50, Calculated by the dose- dependent proliferation of mouse BALB/c 3T3 cells is < 0.05ng/ml corresponding to a specific activity of 2.0x107 units/mg.
What is the amino acid sequence of FGF 2 Protein?
MPALPEDGGS GAFPPGHFKD PKRLYCKNGG FFLRIHPDGR VDGVREKSDP HIKLQLQAEE RGVVSIKGVC ANRYLAMKED GRLLASKCVT DECFFFERLE SNNYNTYRSR KYTSWYVALK RTGQYKLGSK TGPGQKAILF LPMSAKS.
What applications can FGF 2 Protein be used in?
FGF 2 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF 2 Protein?
The endotoxin level is minimal, FGF 2 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 :
Leptin Mouse, PEGDescription:
Pegylated Mouse Leptin Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-591Price :
Quantity :
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Shipped at Room temp
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Description
Leptin Mono-Pegylated Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and an additional Ala at N-terminus. Pegylated Mouse Leptin contains PEG 20 kDa at its N-terminus and having a molecular mass of 35.6 kDa as determined by mass spectrometry. Since its enlarged hydrodymanic volume Pegylated Leptin runs on SDS-PAGE as A 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein. Pegylated Mouse Leptin half-life in circulation after SC injection was over 20 hours. Mouse Leptin was purified by proprietary chromatographic techniques according to Salomon et al (2006) Protein Expression and Purification 47, 128–136 and then pegylated.
Source
Escherichia Coli.
Formulation
The mouse Leptin was lyophilized from a concentrated (0.65mg/ml) solution containing 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Analysis by Gel-Filtration.
(b) Analysis by SDS-PAGE.Biological Activity
Pegylated mouse Leptin is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated mouse Leptin in vitro activity is only slightly lower than the non-pegylated antagonist but in vivo it has profound weight reducing effect (as compared to the non-pegylated leptin), resulting mainly from reduced food intake.More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin in sterile 0.4% NaHCO3 adjusted to pH-8.5 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SNAP25 C.elegansDescription:
Synaptosomal-associated protein 25kDa C.elegans Recombinant
Super-Protein, SUP, RIC4, SEC9, SNAP, RIC-4, SNAP25, SNAP-25, Synaptosomal-associated protein 25, Synaptosomal-associated 25 kDa protein, FLJ23079, bA416N4.2, dJ1068F16.2.
Product # :
PRO-396Price :
Quantity :
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Shipped with Ice Packs
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Description
Recombinant C.elegans SNAP-25 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids and having a molecular mass of 23kDa. SNAP-25 gene was amplified by PCR from C.elegans and cloned into an E. coli expression vector. SNAP-25 was purified by using conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The protein contains 20mM Tris-HCl pH7.5, 50mM NaCl, 5mM DTT, 1mM EDTA and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Synaptic vesicle membrane docking and fusion is mediated by SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) located on the vesicle membrane (v-SNAREs) and the target membrane (t-SNAREs). The assembled v-SNARE/t-SNARE complex consists of a bundle of four helices, one of which is supplied by v-SNARE and the other three by t-SNARE. For t-SNAREs on the plasma membrane, the protein syntaxin supplies one helix and the protein encoded by this gene contributes the other two. Therefore, SNAP25 product is a presynaptic plasma membrane protein involved in the regulation of neurotransmitter release. The synaptosomal-associated protein (SNAP-25) is an essential component of the core complex that mediates presynaptic vesicle trafficking. Thus, SNAP-25 is directly involved in the release of neurotransmitters.
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Synonyms
Super-Protein, SUP, RIC4, SEC9, SNAP, RIC-4, SNAP25, SNAP-25, Synaptosomal-associated protein 25, Synaptosomal-associated 25 kDa protein, FLJ23079, bA416N4.2, dJ1068F16.2.
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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
MSGDDDIPEG LEAINLKMNA TTDDSLESTR RMLALCEESK EAGIKTLVML DDQGEQLERCEGALDTINQD MKEAEDHLKG MEKCCGLCVL PWNKTDDFEK TEFAKAWKKD DDGGVISDQPRITVGDSSMG PQGGYITKIT NDAREDEMDE NVQQVSTMVG NLRNMAIDMS TEVSNQNRQL DRIHDKAQSN EVRVESANKR AKNLITK.
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 :
STX11 HumanDescription:
Syntaxin-11 Human Recombinant
Syntaxin-11, STX11, FHL4, HLH4, HPLH4.
Product # :
PRO-1111Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
STX11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 311 amino acids (1-287 a.a) and having a molecular mass of 35.8kDa.STX11 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
STX11 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Syntaxin-11 (STX11) belongs to the t-SNARE family. Syntaxin-11 regulates protein transport between late endosomes and the trans-Golgi network. STX11 interacts with the SNARE proteins SNAP-23 and VAMP. STX11 gene mutations are linked with familial hemophagocytic lymphohistiocytosis.
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Synonyms
Syntaxin-11, STX11, FHL4, HLH4, HPLH4.
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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 MGSHMKDRLA ELLDLSKQYD QQFPDGDDEF DSPHEDIVFE TDHILESLYR DIRDIQDENQ LLVADVKRLG KQNARFLTSM RRLSSIKRDT NSIAKAIKAR GEVIHCKLRA MKELSEAAEA QHGPHSAVAR ISRAQYNALT LTFQRAMHDY NQAEMKQRDN CKIRIQRQLE IMGKEVSGDQ IEDMFEQGKW DVFSENLLAD VKGARAALNE IESRHRELLR LESRIRDVHE LFLQMAVLVE KQADTLNVIE LNVQKTVDYT GQAKAQVRKA VQYEEKNPCR TLCCFCCPCL K.
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 :
TFF2 HumanDescription:
Trefoil Factor-2 Human Recombinant
TFF-2, Spasmolytic polypeptide, Spasmolysin, SML1, Trefoil factor 2, SP, TFF2.
Product # :
CYT-612Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TFF-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 106 amino acids (24-129) and having a total molecular mass of 12 kDa. TFF2 Human Recombinant includes a 40-amino acid trefoil motif containing three conserved intramolecular disulfide bonds and was purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TFF2 protein was lyophilized from 0.4μm filtered solution at a concentration of 1mg/mL 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
Determined by its ability to chemoattract human MCF-7 cells using a concentration 1.0-10.0 ng/ml.More Info
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Introduction
Proteins of the TFF family are characterized by obtaining a minimum of 1 copy of the trefoil motif, a 40-amino acid domain that contains 3 conserved disulfides. Trefoil Factors are stable secretory proteins expressed in gastrointestinal mucosa which protect the mucosa from insults, stabilize the mucus layer and affect healing of the epithelium.TFF2 inhibits gastric acid motility & secretion. TFF2 stabilizes glycoproteins in the mucus gel through interactions with carbohydrate side chains.
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Synonyms
TFF-2, Spasmolytic polypeptide, Spasmolysin, SML1, Trefoil factor 2, SP, TFF2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TFF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF2 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 TFF2 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
EKPSPCQCSR LSPHNRTNCG FPGITSDQCF DNGCCFDSSV TGVPWCFHPL PKQESDQCVM EVSDRRNCGY PGISPEECAS RKCCFSNFIF EVPWCFFPKSVEDCHY.
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 :
CCL28 Human, HisDescription:
Mucosae-Associated Epithelial Chemokine Human Recombinant (CCL28), His Tag
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
Product # :
CHM-366Price :
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Shipped with Ice Packs
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Description
CCL28 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 126 amino acids (23-127 a.a.) and having a molecular mass of 14.3 kDa. The CCL28 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CCL28 protein contains 10mM Sodium Citrate pH3.5 and 10% Glycerol.
Purity
Greater than 90% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues. -
Synonyms
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
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Physical Appearance
Sterile filtered 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 MILPIASSCC TEVSHHISRR LLERVNMCRI QRADGDCDLA AVILHVKRRR ICVSPHNHTV KQWMKVQAAK KNGKGNVCHR KKHHGKRNSN RAHQGKHETY GHKTPY.
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Background
What is the molecular weight/Mw of CCL28 HUMAN, HIS Protein?
CCL28 HUMAN, HIS Protein has a total Mw of 14.3kDa.
What is the source or expression system of CCL28 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CCL28 HUMAN, HIS Protein?
CCL28 HUMAN, HIS Protein is > 90% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL28 HUMAN, HIS Protein?
The biological functionality of CCL28 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CCL28 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MILPIASSCC TEVSHHISRR LLERVNMCRI QRADGDCDLA AVILHVKRRR ICVSPHNHTV KQWMKVQAAK KNGKGNVCHR KKHHGKRNSN RAHQGKHETY GHKTPY.
What applications can CCL28 HUMAN, HIS Protein be used in?
CCL28 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL28 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL28 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
Description:
Leptin Super Antagonist Human Recombinant
Product # :
CYT-1238Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Super Leptin Antagonist Human Recombinant is a single polypeptide chain containing 146 amino acids. Super Human Leptin Antagonist was mutated, resulting in D23L/L39A/D40A/F41A super human leptin antagonist that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
ProSpec’s super human leptin antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin.
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Super Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of super human leptin antagonist at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization super human leptin antagonist can be stored at 4C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Super Leptin Antagonist in sterile 0.4% NaHCO3 adjusted to pH 8-9, 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-Val-Pro-Ile-Gln.
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Background
Leptin is a hormone which takes part in regulating body weight, metabolism and reproductive function. Leptin is a~16 kDa protein which is encoded by the obese gene. leptin is expressed predominantly by adipocytes, which fits with the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.
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 :
Vaspin HumanDescription:
Vaspin Recombinant Human
Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.
Product # :
CYT-1132Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Vaspin Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 394 amino acids and having a molecular mass of 45.1kDa. Vaspin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 150mM NaCl and 0.02 % Tween-20.
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
Vaspin (visceral adipose-specific SERPIN) is a newly identified adipokine, which is a member of serine protease inhibitor family. Vaspin is also a unique insulin sensitizing adipocytokine in obesity. A recent publication indicates that induction of human vaspin mRNA expression in adipose tissue is regulated in a fat depot-specific manner and could be associated with parameters of obesity, insulin resistance, and glucose metabolism.
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Synonyms
Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Vaspin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Vaspin 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 Vaspin 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
LKPSFSPRNY KALSEVQGWK QRMAAKELAR QNMDLGFKLL KKLAFYNPGR NIFLSPLSIS TAFSMLCLGA QDSTLDEIKQ GFNFRKMPEK DLHEGFHYII HELTQKTQDL KLSIGNTLFI DQRLQPQRKF LEDAKNFYSA ETILTNFQNL EMAQKQINDF ISQKTHGKIN NLIENIDPGT VMLLANYIFF RARWKHEFDP NVTKEEDFFL EKNSSVKVPM MFRSGIYQVG YDDKLSCTIL EIPYQKNITA IFILPDEGKL KHLEKGLQVD TFSRWKTLLS RRVVDVSVPR LHMTGTFDLK KTLSYIGVSK IFEEHGDLTK IAPHRSLKVG EAVHKAELKM DERGTEGAAG TGAQTLPMET PLVVKIDKPY LLLIYSEKIP SVLFLGKIVN PIGK.
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 :
RCAN2 HumanDescription:
Regulator of Calcineurin 2 Human Recombinant
Regulator of calcineurin 2, DSCR1L1, MCIP2, Down syndrome critical region gene 1-like 1, ZAKI4, Myocyte-enriched calcineurin-interacting protein 2, Thyroid hormone-responsive protein ZAKI-4, CSP2, RCN2, thyroid hormone-responsive (skin fibroblasts).
Product # :
PRO-990Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RCAN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids (1-197 a.a.) and having a molecular mass of 24.1kDa.RCAN2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
RCAN2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 200mM NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
RCAN2 is a member of the RCAN (Regulator of calcineurin) family that controls the activity of Calcineurin using a valine-rich region placed in their carboxyl tail. RCANs race against NFAT (nuclear factor of activated T-cells) to bind to the same docking site in calcineurin, and consequently inhibits or activates calcineurin activity. RCAN2 is a Ca(2+) dependent protein phosphatase which takes part in numerous neuornal functions.
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Synonyms
Regulator of calcineurin 2, DSCR1L1, MCIP2, Down syndrome critical region gene 1-like 1, ZAKI4, Myocyte-enriched calcineurin-interacting protein 2, Thyroid hormone-responsive protein ZAKI-4, CSP2, RCN2, thyroid hormone-responsive (skin fibroblasts).
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPAPSMDCDV STLVACVVDV EVFTNQEVKE KFEGLFRTYD DCVTFQLFKS FRRVRINFSN PKSAARARIE LHETQFRGKK LKLYFAQVQT PETDGDKLHL APPQPAKQFL ISPPSSPPVG WQPINDATPV LNYDLLYAVA KLGPGEKYEL HAGTESTPSV VVHVCDSDIE EEEDPKTSPK PKIIQTRRPG LPPSVSN
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
REG1A HumanDescription:
Regenerating Islet-Derived 1 Alpha Human Recombinant
Lithostathine-1-alpha, Pancreatic stone protein, PSP, Pancreatic thread protein, PTP, Islet of Langerhans regenerating protein, REG, Regenerating protein I alpha, Islet cells regeneration factor, ICRF, REG1A, PSPS, P19, PSPS1, MGC12447.
Product # :
PRO-289Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Recombinant Human REG 1 alpha is produced with N-terminal fusion His Tag. The Recombinant Human REG 1 alpha His-Tagged Fusion Protein, has a molecular weight of 17.8 kDa protein containing 144 amino acid residues of the Human REG 1 alpha and 12 additional amino acid residues – His Tag.
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 5mM Tris, 25mM NaCl, pH 7.5.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
REG protein was shown to be stimulated during the regeneration of pancreatic islets. Since then, many Reg-related proteins have been identified in humans and other animals. In human, the four REG family genes, i.e., REG 1 alpha, REG 1 beta, REG-related sequence (RS) and HIP/PAP, have so far been isolated. These Reg-related proteins are classified into four subfamilies according to their amino-acid sequences, but they share a similar structure and physiological function. Reg protein is a growth factor for pancreatic beta cells and also suggests that the administration of Reg protein could be used as another therapeutic approach for diabetes mellitus. Human REG cDNA which encodes a 166-amino acid protein with a 22-amino acid signal peptide. The amino acid sequence of human REG protein has 68% homology to that of rat Reg protein.
Reg I was found to be expressed mainly in pancreatic beta and acinoductular cells as well as gastric fundic enterochromaffin-like (ECL) cells. Reg I production in ECL cells is stimulated by gastrin, as well as by the proinflammatory cytokine, cytokine-induced neutrophil chemoattractant (CINC)-2Beta. In patients with chronic hypergastrinemia, Reg production is stimulated, with the increased proliferation of gastric mucosal cells. Patients with Helicobacter pylori infection also showed increased Reg production in the gastric mucosa, partly via increased plasma gastrin concentration and partly via increased proinflammatory cytokine production. The serum concentration of the reg-protein was significantly higher in patients with various pancreatic diseases than in normal controls, and was also significantly higher in patients with acute pancreatitis or chronic relapsing pancreatitis than in patients with chronic pancreatitis. Furthermore, the serum PSP/reg-protein concentration was also significantly increased in liver cirrhosis, choledocholithiasis, and various cancers of the digestive system. -
Synonyms
Lithostathine-1-alpha, Pancreatic stone protein, PSP, Pancreatic thread protein, PTP, Islet of Langerhans regenerating protein, REG, Regenerating protein I alpha, Islet cells regeneration factor, ICRF, REG1A, PSPS, P19, PSPS1, MGC12447.
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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
Add deionized water to a working concentration approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS HMQEAQTELP QARISCPEGT NAYRSYCYYF NEDRETWVDA DLYCQNMNSG NLVSVLTQAE GAFVASLIKE SGTDDFNVWI GLHDPKKNRR WHWSSGSLVS YKSWGIGAPS SVNPGYCVSL TSSTGFQKWK DVPCEDKFSF VCKFKN.
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 :
GlucagonDescription:
Glucagon Human
GLP1, GLP2, GRPP.
Product # :
HOR-286Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Glucagon Human Synthetic is a single, non-glycosylated, polypeptide chain containing 29 amino acids and having a molecular mass of 3483 Dalton and the molecular formula is: C153H225N43O49S.The Glucagon is purified by proprietary chromatographic techniques.
Formulation
Glucagon peptide was formulated with no additives.
Purity
Greater than 96.0% as determined by RP-HPLC.
More Info
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Introduction
Glucagon is an important hormone involved in carbohydrate metabolism. The hormone is synthesized and secreted from alpha cells (?-cells) of the islets of Langerhans, which are located in the endocrine portion of the pancreas. Glucagon is released when the glucose level in the blood is low (hypoglycemia), causing the liver to convert stored glycogen into glucose and release it into the bloodstream. The action of glucagon is thus opposite to that of insulin, which instructs the body's cells to take in glucose from the blood in times of satiation.
Glucagon is beneficial for the culture of some cell types. It has been used in some biochemical regulation studies of glycogenolysis in hepatocytes. It has been also been found to induce DNA replication in primary cultures of adult rat hepatocytes when used in combinations with EGF and Insulin. Glucagon increases the blood glucose concentration by promoting rapid breakdown of liver glycogen, and also acts to relax smooth muscle such as the gastrointestinal tract. -
Synonyms
GLP1, GLP2, GRPP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Glucagon although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Glucagon 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 Glucagon in a sterile 1% HCl solution at a concentration of 0.1-1 mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
His-Ser-Gln-Gly-Thr-Phe-Thr-Ser-Asp-Tyr-Ser-Lys-Tyr-Leu-Asp-Ser-Arg-Arg-Ala-Gln-Asp-Phe-Val-Gln-Trp-Leu-Met-Asn-Thr-OH.
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 :
Leptin PufferfishDescription:
Leptin Pufferfish Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-530Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Pufferfish (Takifugu rubripes) Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 16 kDa. Bioactive Leptin Pufferfish (Takifugu rubripes) Recombinant was prepared according to the sequence published by Kurokawa et al. (2005)Peptides 26, 745-750 in two forms: monomer and covalent dimer. MS analysis revealed molecular masses of 15,291 and 30,585 Da, close to the theoretical values of 15,270 and 30,540 Da. CD spectra revealed high similarity to mammalian leptins. Other details of its preparation will be soon published by Yacobovitz et al (in press), General and Comparative Endocrinology.The Pufferfish Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Pufferfish Leptin was lyophilized from a concentrated (0.85mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. The affinity of human leptin receptors is considerably lower campared to mammalian leptins.More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Pufferfish Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Pufferfish Leptin in sterile 0.4% NaHCO3 pH-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
ALPGALDAMDVEKMKSKVTWKAQGLVARIDKHFPDRGLRFDTDKVE
GSTSVVASLESYNNLISDRFGGVSQIKTEISSLAGYLNHWREGNCQE
QQPKVWPRRNIFNHTVSLEALMRVREFLKLLQKNVDLLERC
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 1.28 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
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 :
Leptin Rat, PEGDescription:
Pegylated Rat Leptin Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-592Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Mono-Pegylated Leptin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and an additional Ala at N-terminus having a molecular mass of 35.6 kDa (with 20 kDa PEG) as determined by mass spectometry. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein. Its half-life in circulation after SC injection was over 20 hours. Rat Leptin was purified by proprietary chromatographic techniques according to Salomon et al (2006) Protein Expression and Purification 47, 128–136 and then pegylated.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Analysis by Gel-Filtration.
(b) Analysis by SDS-PAGE.Biological Activity
Pegylated Rat Leptin is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is only slightly lower than the non-pegylated antagonist but in vivo it has profound weight reducing effect (as compared to the non-pegylated leptin), resulting mainly from reduced food intake.More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized pegylated Rat Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of pegylated Rat Leptin at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization Rat leptin can be stored at 4C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized pegylated Rat Leptin in sterile water or in sterile 0.4% NaHCO3 adjusted to pH-8.5, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SCGB1A1 Human, HisDescription:
Uteroglobin Human Recombinant, His Tag
Uteroglobin, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, Secretoglobin family 1A member 1, Urinary protein 1, UP-1, UP1, Urine protein 1, SCGB1A1, CCSP, UGB, CC16.
Product # :
CYT-752Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Uteroglobin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 80 amino acids and including a 10 a.a N-terminal His tag. The total molecular mass is 9.2kDa (calculated).
Source
Escherichia Coli.
Formulation
Filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Uteroglobin (SCGB1A1) which belongs to the Secretoglobin (SCGBs) superfamily, is a multifunctional protein that exerts anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules such as phospholipids and prostaglandins. Uteroglobin is involved in numerous functions including anti-inflammation, inhibition of phospholipase A2 and the sequestering of hydrophobic ligands. SCGB1A1 is expressed by Clara cells, the non-ciliated, non-mucous secretory cells predominant in lung bronchioles, and by other epithelia which communicate with the external environment. On top of sequestering pro-inflammatory mediators and carcinogens, Uteroglobin is implicated in the inhibition of cell migration and invasion, platelet aggregation, and T cell differentiation. SCGB1A1 gene defects are associated with a susceptibility to asthma.
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Synonyms
Uteroglobin, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, Secretoglobin family 1A member 1, Urinary protein 1, UP-1, UP1, Urine protein 1, SCGB1A1, CCSP, UGB, CC16.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. SCGB1A1 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
MKHHHHHHASEICPSFQRVI ETLLMDTPSS YEAAMELFSP DQDMREAGAQ LKKLVDTLPQ KPRESIIKLM EKIAQSSLCN.
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 :
Gliadin NativeDescription:
Gliadin Triticum Aestivum Grain Native
Product # :
PRO-2675Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
The native Gliadin Triticum Aestivum Grain is purified from wheat by protein chemical methods.
Formulation
Gliadin is supplied in 20mM HEPES buffer pH-7.4 and 6M Urea.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Gliadin is a common substrate of transglutaminase, which generates neo-epitopes by deamidation of glutamine side chains. In the past, serologic tests for gliadin antibodies usually were not very precise and were not enough for accurate diagnosis due to missing deamidated epitopes within the authentic gliadin fraction traditionally used in diagnostic test kits. ProSpec's deamidated Gliadin isoform matches to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation.
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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. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG and IgA-type human auto antibodies in sera of patients diagnosed with celiac disease.2. Immunodot analysis with positive/negative samples.
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Applications
Western blot with patient sample.
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 :
SSSCA1 HumanDescription:
Sjogren Syndrome/Scleroderma Autoantigen 1 Human Recombinant
Sjogren Syndrome/Scleroderma Autoantigen 1, Sjogren'S Syndrome/Scleroderma Autoantigen 1, Autoantigen P27, Centromeric Autoantigen (27kD), p27, Sjoegren Syndrome/Scleroderma Autoantigen 1.
Product # :
PRO-1743Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SSSCA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (1-199aa) and having a molecular mass of 23.9kDa. SSSCA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SSSCA1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Sjogren syndrome/scleroderma autoantigen 1, SSSCA1 is involved in mitosis. SSSCA1 is a centromere-associated protein which can induce anti-centromere antibodies. In addition SSSCA1 is recognized by a subset of anti-centromere antibodies from patients with sclerodermaand Sjogren's syndrome.
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Synonyms
Sjogren Syndrome/Scleroderma Autoantigen 1, Sjogren'S Syndrome/Scleroderma Autoantigen 1, Autoantigen P27, Centromeric Autoantigen (27kD), p27, Sjoegren Syndrome/Scleroderma Autoantigen 1.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMALNGAE VDDFSWEPPT EAETKVLQAR RERQDRISRL MGDYLLRGYR MLGETCADCG TILLQDKQRK IYCVACQELD SDVDKDNPAL NAQAALSQAR EHQLASASEL PLGSRPAPQP PVPRPEHCEG AAAGLKAAQG PPAPAVPPNT DVMACTQTAL LQKLTWASAE LGSSTSLETS IQLCGLIRAC AEALRSLQQL QH
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 :
AlarelinDescription:
Alarelin
Alarelin, Alarelin Acetate.
Product # :
HOR-291Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Alarelin acetate peptide is a single, non-glycosylated polypeptide chain containing 9 amino acids, having a molecular mass of 1167.3 Dalton and a Molecular formula of C56H78N16O12 x C2H4O2. The CAS No. is 79561-22-1.
Formulation
The Alarelin was lyophilized with no additives.
Purity
Greater than 99.0% as determined by Analysis by RP-HPLC.
More Info
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Introduction
Alarelin (Gonadotrophin-releasing hormone) is a synthetic LH-RH agonist that is found in higher amounts than that of LH-RH in rat hypophyseal stimulation of gonadotropin secretion in vivo and in vitro and in ovulation inductions. Alarelin is known for its induction of ovulation. Alarelin acetate is the acetate form of a hypothalamic peptide that stimulates the release of FSH and LH from the pituitary gland.
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Synonyms
Alarelin, Alarelin Acetate.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Alarelin e although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Alarelin 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 Argipressin 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
5-oxo-pro-His-Trp-Ser-Tyr-D-Ala-Leu-Arg-Pro-Nhet x CH3COOH.
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 :
SERPINI1 Human, HisDescription:
Serpin Peptidase Inhibitor, Clade I Member 1 Human Recombinant, His Tag
Neuroserpin, Peptidase inhibitor 12, PI-12, Serpin I1, SERPINI1, PI12.
Product # :
PRO-1595Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
SERPINI1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 17-410) containing 404 amino acids and including a 10 a.a N-terminal His tag. The total molecular mass is 45.9kDa (calculated).
Source
Escherichia Coli.
Formulation
Filtered (0.4 µm) and lyophilized from 0.5mg/ml in 0.025M phosphate buffer and 0.035M NaCl, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
SERPINI1 (Neuroserpin) is an inhibitory serpin which is expressed primarily in the central nervous system. Even though the physiological target of SERPINI1 is still vague, amassed evidence suggest that SERPINI1 has an imperative role in controlling proteolytic degradation of extracellular matrix (ECM) during synaptogenesis and the subsequent development of neuronal plasticity. The neuroprotective role of SERPINI1 has been demonstrated in transgenic mice lacking SERPINI1 expression. The deficiency of SERPINI1 in these mice is linked with motor neuron disease characterized by axonal degradation. In humans, defects in SERPINI1, caused by point mutations in the neuroserpin gene, trigger a hereditary disorder known as the familial encephalopathy with neuroserpin inclusion bodies (FENIB).
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Synonyms
Neuroserpin, Peptidase inhibitor 12, PI-12, Serpin I1, SERPINI1, PI12.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. SERPINI1 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
MKHHHHHHASTGATFPEEAI ADLSVNMYNR LRATGEDENI LFSPLSIALA MGMMELGAQG STQKEIRHSM GYDSLKNGEE FSFLKEFSNM VTAKESQYVM KIANSLFVQN GFHVNEEFLQ MMKKYFNAAV NHVDFSQNVA VANYINKWVE NNTNNLVKDL VSPRDFDAAT YLALINAVYF KGNWKSQFRP ENTRTFSFTK DDESEVQIPM MYQQGEFYYG EFSDGSNEAG GIYQVLEIPY EGDEISMMLV LSRQEVPLAT LEPLVKAQLV EEWANSVKKQ KVEVYLPRFT VEQEIDLKDV LKALGITEIF IKDANLTGLS DNKEIFLSKA IHKSFLEVNE EGSEAAAVSG MIAISRMAVL YPQVIVDHPF FFLIRNRRTG TILFMGRVMH PETMNTSGHD FEEL.
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 :
NRG4 HumanDescription:
Neuregulin-4 Human Recombinant
Neuregulin 4, HRG4, Pro-neuregulin-4, membrane-bound isoform, Pro-NRG4, NRG-4.
Product # :
CYT-808Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NRG4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 84 amino acids (1-61 a.a.) and having a molecular mass of 9.1kDa. NRG4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NRG4 protein solution (0.25mg/ml) contains 20mM Tris-HCl(pH8.0), 30% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Neuregulin-4 (NRG4) is a part of the neuregulin family that owns 1 EGF-like domain and is a low affinity ligand for the ERBB4 tyrosine kinase receptor. NRG4 links ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors.
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Synonyms
Neuregulin 4, HRG4, Pro-neuregulin-4, membrane-bound isoform, Pro-NRG4, NRG-4.
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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 MGSMPTDHEE PCGPSHKSFC LNGGLCYVIP TIPSPFCRCV ENYTGARCEE VFLPGSSIQT KSNL.
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 :
SPINT2 Human, Sf9Description:
Serine Peptidase Inhibitor, Kunitz Type 2 Human Recombinant, Sf9
Serine Peptidase Inhibitor, Kunitz Type, 2, Placental Bikunin, Hepatocyte Growth Factor Activator Inhibitor Type 2, Serine Protease Inhibitor, Kunitz Type, 2, HAI-2, HAI2, Kop, Kunitz-Type Protease Inhibitor 2, Placental, Bikunin, DIAR3, PB, Kunitz-type protease inhibitor 2.
Product # :
PRO-2219Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SPINT2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 176 amino acids (28-197 a.a.) and having a molecular mass of 20kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). SPINT2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SPINT2 protein solution (0.2mg/ml) contains phosphate buffered saline (pH 7.4) and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
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Introduction
SPINT2 is a transmembrane protein acts as an inhibitor of HGF activator. SPINT2 inhibits plasmin, plasma and tissue kallikrein, and factor XIa. SPINT2 has two extracellular Kunitz domains that inhibit few serine proteases. SPINT2 is assumed tumor suppressor, mutations in SPINT2 leads to a congenital sodium diarrhea.
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Synonyms
Serine Peptidase Inhibitor, Kunitz Type, 2, Placental Bikunin, Hepatocyte Growth Factor Activator Inhibitor Type 2, Serine Protease Inhibitor, Kunitz Type, 2, HAI-2, HAI2, Kop, Kunitz-Type Protease Inhibitor 2, Placental, Bikunin, DIAR3, PB, Kunitz-type protease inhibitor 2.
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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
ADRERSIHDF CLVSKVVGRC RASMPRWWYN VTDGSCQLFV YGGCDGNSNN YLTKEECLKK CATVTENATG DLATSRNAAD SSVPSAPRRQ DSEDHSSDMF NYEEYCTANA VTGPCRASFP RWYFDVERNS CNNFIYGGCR GNKNSYRSEE ACMLRCFRQQ ENPPLPLGSK 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.
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Name :
Periostin Human, HEKDescription:
Periostin Human Recombinant, HEK
OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.
Product # :
CYT-835Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Periostin Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn22-Gln836) containing a total of 821 amino acids, having a calculated molecular mass of 91.8kDa and fused to a 6 aa His tag at C-Terminus.
Source
HEK 293.
Formulation
Periostin was filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in phosphate buffered saline and 5% trehalose.
Purity
Greater than 38.0% as determined by SDS-PAGE.
More Info
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Introduction
Periostin is a disulfide linked 90 kDa, 811 amino acid protein originally isolated as a osteoblast-specific factor that functions as a cell adhesion molecule for preosteoblasts and is thought to be involved in osteoblast recruitment, attachment and spreading. Additionally, periostin expression has previously been shown to be significantly increased by both transforming growth factor beta-1(TGFbeta1) and bone morphogenetic protein (BMP-2). OSF-2 has a typical signal sequence, followed by a cysteine-rich domain, a fourfold repeated domain and a C-terminal domain. The fourfold repeated domain of OSF-2 shows homology with the insect protein fasciclin
Periostin mRNA is expressed in the developing mouse embryonic and fetal heart, and that it is localized to the endocardial cushions that ultimately divide the primitive heart tube into a four-chambered heart. -
Synonyms
OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.
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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.
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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. Periostin 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
NNHYDKILAH SRIRGRDQGP NVCALQQILG TKKKYFSTCK NWYKKSICGQ KTTVLYECCP GYMRMEGMKG CPAVLPIDHV YGTLGIVGAT TTQRYSDASK LREEIEGKGS FTYFAPSNEA WDNLDSDIRR GLESNVNVEL LNALHSHMIN KRMLTKDLKN GMIIPSMYNN LGLFINHYPN GVVTVNCARI IHGNQIATNG VVHVIDRVLT QIGTSIQDFI EAEDDLSSFR AAAITSDILE ALGRDGHFTL FAPTNEAFEK LPRGVLERIM GDKVASEALM KYHILNTLQC SESIMGGAVF ETLEGNTIEI GCDGDSITVN GIKMVNKKDI VTNNGVIHLI DQVLIPDSAK QVIELAGKQQ TTFTDLVAQL GLASALRPDG EYTLLAPVNN AFSDDTLSMD QRLLKLILQN HILKVKVGLN ELYNGQILET IGGKQLRVFV YRTAVCIENS CMEKGSKQGR NGAIHIFREI IKPAEKSLHE KLKQDKRFST FLSLLEAADL KELLTQPGDW TLFVPTNDAF KGMTSEEKEI LIRDKNALQN IILYHLTPGV FIGKGFEPGV TNILKTTQGS KIFLKEVNDT LLVNELKSKE SDIMTTNGVI HVVDKLLYPA DTPVGNDQLL EILNKLIKYI QIKFVRGSTF KEIPVTVYTT KIITKVVEPK IKVIEGSLQP IIKTEGPTLT KVKIEGEPEF RLIKEGETIT EVIHGEPIIK KYTKIIDGVP VEITEKETRE ERIITGPEIK YTRISTGGGE TEETLKKLLQ EEVTKVTKFI EGGDGHLFED EEIKRLLQGD TPVRKLQANK KVQGSRRRLR EGRSQHHHHH H.
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 :
TUBG1 Human, Sf9Description:
Tubulin Gamma 1 Human Recombinant, Sf9
Tubulin gamma-1 chain, Gamma-1-tubulin, Gamma-tubulin complex component 1, GCP-1, TUBG1, TUBG, Tubulin, Gamma 1, Gamma-1-Tubulin, TUBGCP1, CDCBM4.
Product # :
PRO-2532Price :
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Shipping Method :
Shipped with Ice Packs
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Description
TUBG1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 457 amino acids (1-451 a.a.) and having a molecular mass of 51.9kDa. TUBG1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
TUBG1 protein solution (0.25mg/ml) contains 20mM Tris-HCl (pH 8.0) containing 40% glycerol, 0.1M NaCl,2mM DTT and 50mM imidazole.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
TUBG1 belongs to the tubulin superfamily. TUBG1 localizes to the centrosome and binds to microtubules to create the gamma-tubulin ring complex. TUBG1 facilitates the microtubule nucleation and is essential for microtubule formation and progression of the cell cycle.
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Synonyms
Tubulin gamma-1 chain, Gamma-1-tubulin, Gamma-tubulin complex component 1, GCP-1, TUBG1, TUBG, Tubulin, Gamma 1, Gamma-1-Tubulin, TUBGCP1, CDCBM4.
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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
MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY IPRAVLLDLE PRVIHSILNS PYAKLYNPEN IYLSEHGGGA GNNWASGFSQ GEKIHEDIFD IIDREADGSD SLEGFVLCHS IAGGTGSGLG SYLLERLNDR YPKKLVQTYS VFPNQDEMSD VVVQPYNSLL TLKRLTQNAD CVVVLDNTAL NRIATDRLHI QNPSFSQINQ LVSTIMSAST TTLRYPGYMN NDLIGLIASL IPTPRLHFLM TGYTPLTTDQ SVASVRKTTV LDVMRRLLQP KNVMVSTGRD RQTNHCYIAI LNIIQGEVDP TQVHKSLQRI RERKLANFIP WGPASIQVAL SRKSPYLPSA HRVSGLMMAN HTSISSLFER TCRQYDKLRK REAFLEQFRK EDMFKDNFDE MDTSREIVQQ LIDEYHAATR PDYISWGTQE QHHHHHH.
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.