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1000 results found for “secretogranin”
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- View Data Sheet
Name :
Gliadin Gamma 18.6kDa WheatDescription:
Gliadin Gamma 18.6kD Wheat Recombinant
Product # :
PRO-114Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Gliadin is a cDNA coding for an epitope-carrying fragment of a wheat gamma-gliadin isoform, having a molecular mass of 19 kDa (high proline content and the low pI are likely causes for the observed discrepancy between calculated molecular weight and the observed electrophoretic mobility of approx. 50 kDa on standard SDS-PAGE), pH 4.6. By sequence design the epitopes correspond to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation. Gliadin protein is fused to a hexa-histidine purification tag.
Source
Escherichia Coli.
Formulation
Gliadin is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl, and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Wheat Gliadin and related gluten components from barley, rye and possibly oats can cause an abnormal immune response called Celiac disease which is a chronic gastrointestinal disorder. Celiac disease characteristics are flattening of the jejunal mucosa and intestinal lesions of variable severity in hereditarily inclined individuals. Even though Celiac disease is not a classic autoimmune disease it is related to anti-tissue transglutaminase antibodies and gliadin antibodies tests are most recommended in screening populations at risk for CD and other gluten-sensitive enteropathies. 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 autoantibodies associated with celiac disease. 2. Standard ELISA test (checkerboard analysis of positive/negative sera panels); immunodot.
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coating concentration
0.15-0.5 µg/ml (depending on the type of ELISA plate and coating buffer).
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Applications
Western blot with monoclonal anti-hexa-His-tag antibody.
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 :
LGALS2 Mouse, ActiveDescription:
Galectin-2, BioActive Mouse Recombinant
Galectin-2, Gal-2, Lgals2, 2200008F12Rik, AI324147.
Product # :
CYT-1155Price :
Quantity :
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Shipped with Ice Packs
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Description
LGALS2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids (1-130 a.a) and having a molecular mass of 17.3kDa.LGALS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
LGALS2 protein (1mg/ml) contains 10% glycerol, 0.1M NaCl, 1mM DTT and 20mM Tris-HCl buffer (pH 8.0).
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Measured by its ability to agglutinate human red blood cells. The ED50 is ≥ 20ug/ml.
More Info
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Introduction
Galectin-2 or LGALS2 is a protein, part of the galectin proteins family. The galectin proteins family holds galectin proteins family lectins that mediates adhesion between cells or cells to ECM. This family also take part in pre-mRNA splicing, apoptosis & tumor progression. Galectin-2 induces apoptosis in T cells that are activated & binds to lymphotoxin-a, also can implicatate on myocardial infarction. LGALS2 from human and mouse share about 65% amino acid sequence resemblance.
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Synonyms
Galectin-2, Gal-2, Lgals2, 2200008F12Rik, AI324147.
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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 MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE
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Background
What is the molecular weight/Mw of LGALS2 MOUSE, ACTIVE Protein?
LGALS2 MOUSE, ACTIVE Protein has a total Mw of 17.3kDa.
What is the source or expression system of LGALS2 MOUSE, ACTIVE Protein?
Escherichia Coli.
What is the Purity of LGALS2 MOUSE, ACTIVE Protein?
LGALS2 MOUSE, ACTIVE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS2 MOUSE, ACTIVE Protein?
Measured by its ability to agglutinate human red blood cells. The ED50 is ≥ 20ug/ml.
What is the amino acid sequence of LGALS2 MOUSE, ACTIVE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE.
What applications can LGALS2 MOUSE, ACTIVE Protein be used in?
LGALS2 MOUSE, ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS2 MOUSE, ACTIVE Protein?
The endotoxin level is minimal, LGALS2 MOUSE, ACTIVE 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 ChickenDescription:
Leptin Chicken Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-505Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Chicken Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 145 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 95.0% 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. Its activity is however 5-10 fold lower as compared 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 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 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-Val-Pro-Cys-Gln.
Recombinant Chicken leptin was produced according to the a.a. sequence published by the groups of Taouis & McMutry, see Raver et al. Protein Expr Purif. 1998 Dec; 14(3):403-8.
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Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.19 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC,using calibrated solution of Leptin Chicken as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CRYAB HumanDescription:
Crystallin Alpha B Human Recombinant
CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.
Product # :
HSP-003Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant CRYAB produced in E.Coli is a single,non-glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 20.1kDa. CRYAB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CRYAB protein (1mg/ml) solution contains 20mM Tris-HCl buffer pH-7.5, 50mM NaCl and 1mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Alpha crystallins are composed of two gene products ; alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20). They act as molecular chaperones and hold them in in large soluble aggregates. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional function of a-crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-B is expressed widely in many tissues and organs and occurs in many neurological diseases.
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Synonyms
CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.
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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
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR PPSFLRAPSWFDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHRKYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVT AAPKK.
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 :
HMGA2 HumanDescription:
High Mobility Group AT-Hook 2 Human Recombinant
High Mobility Group AT-Hook 2, HMGIC, High-Mobility Group (Nonhistone Chromosomal) Protein Isoform I-C, High Mobility Group AT-Hook Protein, BABL, HMGI-C, LIPO, STQTL9, High Mobility Group Protein HMGI-C, HMGA2.
Product # :
PRO-1469Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HMGA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 117 amino acids (1-109 a.a) and having a molecular mass of 12.8kDa.HMGA2 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HMGA2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol, 2mM DTT and 250mM Imidazole.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
High Mobility Group AT-Hook 2 (HMGA2) is a member of the non-histone chromosomal high mobility group (HMG) family. HMG proteins perform as architectural factors and are necessary components of the enhancesome. Thisprotein contains structural DNA-binding domains and may function as a transcriptional regulating factor. In addition, identification ofthe deletion, amplification, and rearrangement of this gene that are associated with myxoid liposarcoma proposes arole in adipogenesis and mesenchymal differentiation. A gene knock out study of the mouse counterpartdemonstrated that this gene is implicated in diet-induced obesit.Among the Diseases associated with HMGA2 are diffuse lipomatosis, and 12q14 microdeletion syndrome.
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Synonyms
High Mobility Group AT-Hook 2, HMGIC, High-Mobility Group (Nonhistone Chromosomal) Protein Isoform I-C, High Mobility Group AT-Hook Protein, BABL, HMGI-C, LIPO, STQTL9, High Mobility Group Protein HMGI-C, HMGA2.
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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
MSARGEGAGQ PSTSAQGQPA APAPQKRGRG RPRKQQQEPT GEPSPKRPRG RPKGSKNKSP SKAAQKKAEA TGEKRPRGRP RKWPQQVVQK KPAQEETEET SSQESAEEDL EHHHHHH.
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 :
SERPINA5 Human, ActiveDescription:
Serpin Peptidase Inhibitor, Clade A Member 5 Human Recombinant, Active
Serpin Family A Member 5, Serine (Or Cysteine) Proteinase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 5, Serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 5, Acrosomal Serine Protease Inhibitor 3 4 Protein C Inhibitor, PLANH3, PAI-3, PROCI, PAI3, PCI, Plasminogen Activator Inhibitor III, Plasminogen Activator Inhibitor-3, Plasminogen Activator Inhibitor 3, Plasma Serine Protease Inhibitor, Serpin A5, PCI-B.
Product # :
PRO-2523Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SERPINA5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 408 amino acids (20-406 a.a) and having a molecular mass of 45.9kDa.SERPINA5 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SERPINA5 protein solution (0.5mg/ml) contains 150mM NaCl, 10% glycerol & 20 mM MES buffer (pH6.0).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured by its ability to inhibit Thrombin cleavage of substrate Boc-VPR-AMC. The IC50 for this effect is less or equal to 2 nM.
More Info
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Introduction
SERPINA5 up regulates TAFI activation by inhibiting the protein C activation. SERPINA5 is a significant regulator in the equilibrium between coagulation and fibrinolysis by differentially inhibiting the activation of TAFI and of Protein-C. SERPINA5 belongs to the serpin serine proteinase inhibitor family. SERPINA5 protein inhibits plasminogen activators as well as activated protein C.
SERPINA5 is secreted in plasma & liver. SERPINA5 is involved in cell inflammation, proliferation, apoptosis, tumour cell migration, invasion, and metastasis. Moreover, SERPINA5 controls the invasive potential of renal cell carcinoma by inhibiting urinary plasminogen activator secreted by the cells. SERPINA5 participtes in regulating key serine proteases which are involved in metastatic prostate disease. -
Synonyms
Serpin Family A Member 5, Serine (Or Cysteine) Proteinase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 5, Serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 5, Acrosomal Serine Protease Inhibitor 3 4 Protein C Inhibitor, PLANH3, PAI-3, PROCI, PAI3, PCI, Plasminogen Activator Inhibitor III, Plasminogen Activator Inhibitor-3, Plasminogen Activator Inhibitor 3, Plasma Serine Protease Inhibitor, Serpin A5, PCI-B.
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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 MHRHHPREMK KRVEDLHVGA TVAPSSRRDF TFDLYRALAS AAPSQNIFFS PVSISMSLAM LSLGAGSSTK MQILEGLGLN LQKSSEKELH RGFQQLLQEL NQPRDGFQLS LGNALFTDLV VDLQDTFVSA MKTLYLADTF PTNFRDSAGA MKQINDYVAK QTKGKIVDLL KNLDSNAVVI MVNYIFFKAK WETSFNHKGT QEQDFYVTSE TVVRVPMMSR EDQYHYLLDR NLSCRVVGVP YQGNATALFI LPSEGKMQQV ENGLSEKTLR KWLKMFKKRQ LELYLPKFSI EGSYQLEKVL PSLGISNVFT SHADLSGISN HSNIQVSEMV HKAVVEVDES GTRAAAATGT IFTFRSARLN SQRLVFNRPF LMFIVDNNIL FLGKVNRP.
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 :
ANKRA2 HumanDescription:
Ankyrin Repeat Family A2 Human Recombinant
Ankyrin Repeat, Family A (RFXANK-Like), 2, ANKRA, RFXANK-Like Protein 2, Ankyrin Repeat Family A Protein 2, ANKRA2.
Product # :
PRO-2062Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ANKRA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 336 amino acids (1-313a.a) and having a molecular mass of 36.7kDa. ANKRA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ANKRA2 protein solution (0.25 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Ankyrin Repeat Family A2, also known as ANKRA2 contains 5 ANK repeats. ANKRA2 assist endocytosis by linking megalin to components of the cytoskeleton or endocytic machinery.
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Synonyms
Ankyrin Repeat, Family A (RFXANK-Like), 2, ANKRA, RFXANK-Like Protein 2, Ankyrin Repeat Family A Protein 2, ANKRA2.
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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 MGSMDTSTNL DIGAQLIVEE CPSTYSLTGM PDIKIEHPLD PNSEEGSAQG VAMGMKFILP NRFDMNVCSR FVKSLNEEDS KNIQDQVNSD LEVASVLFKA ECNIHTSPSP GIQVRHVYTP STTKHFSPIK QSTTLTNKHR GNEVSTTPLL ANSLSVHQLA AQGEMLYLAT RIEQENVINH TDEEGFTPLM WAAAHGQIAV VEFLLQNGAD PQLLGKGRES ALSLACSKGY TDIVKMLLDC GVDVNEYDWN GGTPLLYAVH GNHVKCVKML LESGADPTIE TDSGYNSMDL AVALGYRSVQ QVIESHLLKL LQNIKE.
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 :
HTF BovineDescription:
Holo Transferrin Bovine
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.
Product # :
PRO-510Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Bovine Holo Transferrin is a glycoprotein of approximately 80 kDa.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 97.0% as determined by Cellulose Acetate.
More Info
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Introduction
Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity. -
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.
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Physical Appearance
Sterile Filtered Pink lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bovine HTF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Bovine HTF 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 Bovine HTF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Human Virus Test
FDA approved Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HBSAG, HBc, ALT and Syphilis.Viral inactivation by pasteurization (60°C for 10 hours) has been validated using three different test viruses, with removal of 8-14.5 logs of virus documented. The purification process has also been found to remove significant additional quantities of virus.
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Applications
Bovine Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Bovine Transferrin is Critical for long-term cells growth in-vitro. Bovine Transferrin is used as detoxificant in media by binding contaminating metal ions. Bovine Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Bovine Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into 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.
- View Data Sheet
Name :
NRG1 B1 HumanDescription:
Neuregulin-1/Heregulin-b1 Human Recombinant
Neuregulin-1, Heregulin-b1, NRG1-B1, NRG1 B1.
Product # :
CYT-733Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Recombinant Human Neuregulin-1/Heregulin-b1 produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 177-241) containing 65 amino acids and having a total molecular mass of 7.5kDa. NRG1-B1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered solution in 1×PBS, pH 7.4 and 5% trehalose.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 was determined by the dose-dependent stimulation of the proliferation of human MCF-7 cells is less than 0.5ng/ml, corresponding to a specific activity of >2.0×106 units/mg.More Info
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Introduction
Neuregulin/Heregulin is a family of structurally related polypeptide growth factors which are stemmed from alternatively spliced genes (NRG1, NRG2, NRG3 and NRG4). Thus far, there are more than 14 soluble and transmembrane proteins derived from the NRG1 gene. Proteolytic processing of the extracellular domain of the transmembrane NRG1 isoforms release soluble growth factors. HRG1-b1 is comprised of an Ig domain and an EGF-like domain which is necessary for direct binding to receptor tyrosine kinases erb3 and erb4. This binding stimulates erb3 and erb4 heterodimerization with erb2, promoting intrinsic kinase activity, which results in tyrosine phosphorylation. Even though HRG1-b1 biological effects are still unclear, it has been discovered to advance motility and invasiveness of breast cancer cells which in addition might entail up-regulation of expression and function of the autocrine motility-promoting factor (AMF).
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Synonyms
Neuregulin-1, Heregulin-b1, NRG1-B1, NRG1 B1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized NRG1-B1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NRG1-B1 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 NRG1-B1 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
SHLVKCAEKE KTFCVNGGEC FMVKDLSNPS RYLCKCPNEF TGDRCQNYVM ASFYKHLGIE FMEAE.
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 :
OPG Human, Hi-5Description:
Osteoprotegerin Human Recombinant, Hi-5
TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, Osteoprotegerin, TR1, MGC29565.
Product # :
CYT-633Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Osteoprotegerin produced in baculovirus is a signle, glycosylated polypeptide chain containing 389 amino acid residues (22-401 a.a.), having a calculated molecular mass of 44.7 kDa. The Osteoprotegerin is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Hi-5.
Formulation
Osteoprotegerin protein contains PBS pH-7.4 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The ED50 range ≤ 8 ng/ml and is measured by its ability to inhibit cytotoxicity using Jurkat human acute T cell leukemia cells in the presence of 2ng/ml of human TRAIL (CAT# cyt-1014).
More Info
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Introduction
Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.
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Synonyms
TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, Osteoprotegerin, TR1, MGC29565.
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Physical Appearance
Sterile Filtered colorless 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. Please avoid freeze thaw cycles.
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Amino Acid Sequence
ADPETFPPKY LHYDEETSHQ LLCDKCPPGT YLKQHCTAKW KTVCAPCPDH YYTDSWHTSD ECLYCSPVCK ELQYVKQECN RTHNRVCECK EGRYLEIEFC LKHRSCPPGF GVVQAGTPER NTVCKRCPDG FFSNETSSKA PCRKHTNCSV FGLLLTQKGN ATHDNICSGN SESTQKCGID VTLCEEAFFR FAVPTKFTPN WLSVLVDNLP GTKVNAESVE RIKRQHSSQE QTFQLLKLWK HQNKDQDIVK KIIQDIDLCE NSVQRHIGHA NLTFEQLRSL MESLPGKKVG AEDIEKTIKA CKPSDQILKL LSLWRIKNGD QDTLKGLMHA LKHSKTYHFP KTVTQSLKKT IRFLHSFTMY KLYQKLFLEM IGNQVQSVKI SCLSHHHHHH.
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 :
OstreolysinDescription:
Ostreolysin Pleurotus Ostreatus Recombinant
Product # :
PRO-2600Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Pleurotus Ostreatus Ostreolysin Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 137 amino acids and having a molecular mass of 15 kDa. The Ostreolysin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Ostreolysin protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Ostreolysin has potent anti-carcinogenic activity in several colon cancer cell lines.
More Info
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Introduction
Ostreolysin is extracted from Pleurotus ostreatus (oyster mushroom). It is a pore forming protein, which contains a lytic part to both cholesterol and sphingomyelin containing membranes. Because of their cholesterol content and the appearance of ostreolysin in the detergent resistant membranes, ostreolysin is cytotoxic towards the ovary cells of Chinese hamster. It seems that Ostreolysin spots a rich lipid cholesterol phase, presumably the liquid ordered phase.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Pleurotus Ostreatus Ostreolysin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon C between 2-7 days and for future use reconstituted Ostreolysin should be stored at 4°C below -18°C. 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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Solubility
It is recommended to reconstitute the lyophilized Ostreolysin in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The N-terminal amino sequence is Ala-Tyr-Ala-Gln-Trp-Val.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 2.64 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNA-man computer analysis program.
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 :
LCN2 RatDescription:
Neutrophil Gelatinase Associated Lipocalin/Lipocalin-2 Rat Recombinant
Neutrophil gelatinase-associated lipocalin, NGAL, Alpha-2-microglobulin-related protein, Alpha-2U globulin-related protein, Lipocalin-2, Siderocalin LCN2, p25.
Product # :
ENZ-920Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LCN2 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (21-198 a.a) and having a molecular mass of 22.9kDa. LCN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LCN2 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Lipocalin-2 also called Neutrophil Gelatinase Associated Lipocalin (NGAL) belongs to a family of lipocans which include 25 proteins (including a1-microglobulin and b-lactoglobulin), which are characterized by their ability to bind small lipophilic substances in their hydrophobic core. They thereby serve as transporters of substances like retinal, biliverdins & prostaglandins. There are indications that NGAL is involved in modulation of the inflammatory response and is found in the plasma of patients after stroke.
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Synonyms
Neutrophil gelatinase-associated lipocalin, NGAL, Alpha-2-microglobulin-related protein, Alpha-2U globulin-related protein, Lipocalin-2, Siderocalin LCN2, p25.
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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 MGSQDSTQNL IPAPPLISVP LQPGFWTERF QGRWFVVGLA ANAVQKERQS RFTMYSTIYE LQEDNSYNVT SILVRGQGCR YWIRTFVPSS RPGQFTLGNI HSYPQIQSYD VQVADTDYDQ FAMVFFQKTS ENKQYFKVTL YGRTKGLSDE LKERFVSFAK SLGLKDNNIV FSVPTDQCID N.
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 :
Transferrin Human, CHODescription:
Transferrin Human Recombinant, CHO
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
Product # :
PRO-2782Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Human Transferrin produced in CHO cells is a glycosylated, polypeptide chain containing having a molecular mass of 76 kDa. Human Transferrin has homologous C and N-terminal domains, each of which binds one ion of ferric iron.
Source
Chinese Hamster Ovary cells.
Formulation
Transferrin solution contains 0.05% NaN3 and PBS.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
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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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Applications
Immunoassay, cell culture.
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Background
Human recombinant transferrin, a glycoprotein responsible for iron transport in the body, has gained increasing attention in the fields of biomedicine and health sciences. This multifaceted protein serves as an essential carrier of iron and is crucial for cellular growth, immunity, and various physiological processes. Its recombinant form, produced through advanced biotechnological methods, offers several advantages for therapeutic and research purposes. This study aims to provide a comprehensive exploration of human recombinant transferrin, shedding light on its various functions and potential applications in health and biomedicine.
The primary objective of this research is to elucidate the essential role of transferrin in iron homeostasis and its significance for human health. In vitro and in vivo experiments will be conducted to investigate how recombinant transferrin interacts with cellular receptors, regulates iron uptake, and influences cellular proliferation. Understanding these mechanisms is fundamental for deciphering the complexities of iron metabolism and its impact on health and disease.
The second objective is to assess the clinical relevance of human recombinant transferrin in medical interventions. Clinical trials and studies involving individuals with iron-related disorders, such as iron-deficiency anemia, will be conducted to evaluate the efficacy and safety of recombinant transferrin supplementation. These investigations may provide insights into the use of recombinant transferrin as a therapeutic agent in various clinical settings.
The third objective is to explore the broader implications of human recombinant transferrin in biomedicine and research. Research will investigate its potential roles in areas beyond iron transport, such as drug delivery, tissue engineering, and cell culture. Understanding the multifaceted properties of recombinant transferrin may open new avenues for innovative approaches in various medical specialties and scientific research.
By delving into the diverse functions of human recombinant transferrin, this research aims to expand our understanding of its physiological roles and clinical applications. The findings may contribute to the development of innovative strategies for the treatment of iron-related disorders and the advancement of biomedicine and scientific research.
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 :
CRYGS HumanDescription:
Crystallin, Gamma S Human Recombinant
Crystallin gamma S, Gamma-crystallin S, CRYG8, crystallin, gamma 8, Beta-crystallin S.
Product # :
PRO-963Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CRYGS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 202 amino acids (1-178) and having a molecular mass of 23.6 kDa.The CRYGS is fused to a 24 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CRYGS solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Mammalian crystallins which are water soluble structural proteins located in the vertebrate eye are classified in three forms, labeled alpha, beta and gamma. Crystallins, the primary components of the lens, raise the refractive index of the eye all through the accommodation by creating high-molecular weight aggregates that maintain transparency. CRYGS is a monomer that does not aggregate. CRYGS encodes the most substantial gamma-crystallin in adult eye lens tissue. Gamma-crystallins has a part in cataract formation due to aging or mutations in specific genes,
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Synonyms
Crystallin gamma S, Gamma-crystallin S, CRYG8, crystallin, gamma 8, Beta-crystallin S.
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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 MGSHMSKTGT KITFYEDKNF QGRRYDCDCD CADFHTYLSR CNSIKVEGGT WAVYERPNFA GYMYILPQGE YPEYQRWMGL NDRLSSCRAV HLPSGGQYKI QIFEKGDFSG QMYETTEDCP SIMEQFHMRE IHSCKVLEGV WIFYELPNYR GRQYLLDKKE YRKPIDWGAA SPAVQSFRRI VE
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 :
AGR3 HumanDescription:
Anterior Gradient Protein 3 Homolog Human Recombinant
Anterior gradient protein 3 homolog, AG-3, AG3, hAG-3, Breast cancer membrane protein 11, AGR3, BCMP11, UNQ642/PRO1272, HAG3, PDIA18.
Product # :
PRO-242Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
AGR3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (22-166 a.a) and having a molecular mass of 19.5kDa.AGR3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AGR3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Anterior gradient protein 3 homolog precursor (AGR3) is a secreted cytoplasmic protein that is involved in metastasis induction and p53 tumor suppressor inhibition. AGR3 may function as molecular marker and potential therapeutic target for hormone-responsive breast tumors.
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Synonyms
Anterior gradient protein 3 homolog, AG-3, AG3, hAG-3, Breast cancer membrane protein 11, AGR3, BCMP11, UNQ642/PRO1272, HAG3, PDIA18.
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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 MGSMIAIKKE KRPPQTLSRG WGDDITWVQT YEEGLFYAQK SKKPLMVIHH LEDCQYSQAL KKVFAQNEEI QEMAQNKFIM LNLMHETTDK NLSPDGQYVP RIMFVDPSLT VRADIAGRYS NRLYTYEPRD LPLLIENMKK ALRLIQSEL.
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 :
DGCR6 HumanDescription:
DiGeorge Syndrome Critical Region Gene 6 Human Recombinant
DiGeorge syndrome critical region gene 6, Protein DGCR6, DGCR6.
Product # :
PRO-1372Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DGCR6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 243 amino acids (1-220 a.a) and having a molecular mass of 27kDa. DGCR6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
DGCR6 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
DiGeorge syndrome critical region gene 6 (DGCR6) shares homology with the Drosophila melanogaster gonadal protein, that participates in gonadal and germ cell development, and also with the gamma-1 subunit of human laminin. DGCR6 is involved in DiGeorge syndrome pathology and in schizophrenia.
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Synonyms
DiGeorge syndrome critical region gene 6, Protein DGCR6, DGCR6.
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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 MGSMERYAGA LEEVADGARQ QERHYQLLSA LQSLVKELPS SFQQRLSYTT LSDLALALLD GTVFEIVQGL LEIQHLTEKS LYNQRLRLQN EHRVLRQALR QKHQEAQQAC RPHNLPVLQA AQQRELEAVE HRIREEQRAM DQKIVLELDR KVADQQSTLE KAGVAGFYVT TNPQELMLQM NLLELIRKLQ QRGCWAGKAA LGLGGPWQLP AAQCDQKGSP VPP.
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 HumanDescription:
Mucosae-Associated Epithelial Chemokine Human Recombinant (CCL28)
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
Product # :
CHM-353Price :
Quantity :
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Shipped at Room temp
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Description
CCL28 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 108 amino acids and having a molecular mass of 12.3 kDa. The CCL28 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM PBS and 150mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.More Info
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Introduction
CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues. -
Synonyms
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CCL28 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL28 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CCL28 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SEAILPIASS CCTEVSHHIS RRLLERVNMC RIQRADGDCD LAAVILHVKR RRICVSPHNH TVKQWMKVQA AKKNGKGNVC HRKKHHGKRN SNRAHQGKHE TYGHKTPY.
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Background
What is the molecular weight/Mw of CCL28 HUMAN Protein?
CCL28 HUMAN Protein has a total Mw of 12.3kDa.
What is the source or expression system of CCL28 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL28 HUMAN Protein?
CCL28 HUMAN Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL28 HUMAN Protein?
Determined by its ability to chemoattract human lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of CCL28 HUMAN Protein?
SEAILPIASS CCTEVSHHIS RRLLERVNMC RIQRADGDCD LAAVILHVKR RRICVSPHNH TVKQWMKVQA AKKNGKGNVC HRKKHHGKRN SNRAHQGKHE TYGHKTPY.
What applications can CCL28 HUMAN Protein be used in?
CCL28 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL28 HUMAN Protein?
The endotoxin level is minimal, CCL28 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 :
TNFRSF10C HumanDescription:
TRAIL Receptor-3 Human Recombinant
Tumor Necrosis Factor Receptor Superfamily, Member 10c, Decoy Without An , Intracellular Domain, TRAILR3, DCR1, TRID, TNF-Related Apoptosis-Inducing Ligand Receptor, Antagonist Decoy Receptor For TRAIL/Apo-2L, Decoy TRAIL Receptor Without Death Domain, Lymphocyte Inhibitor Of TRAIL, Decoy Receptor,TRAIL-R, LIT,Tumor Necrosis Factor Receptor Superfamily Member 10C, TRAIL Receptor Without an Intracellular Domain, Cytotoxic TRAIL Receptor, TRAIL Receptor, CD263 Antigen, DCR1-TNFR, CD263.
Product # :
CYT-889Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TNFRSF10C Human Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 234 amino acids (26-236 a.a) and having a molecular mass of 24.6 kDa.TNFRSF10C is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TNFRSF10C protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
TRAIL Receptor-3, also known as TNFRSF10C belongs to theTNF-receptor super family. TNFRSF10C contains an extracellular TRAIL-binding domain as well as a transmembranedomain, however no cytoplasmic death domain. Furthermore, TNFRSF10C is not capable of inducing apoptosis, and is considered toact as an antagonistic receptor which protects cells from TRAIL-induced apoptosis.
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Synonyms
Tumor Necrosis Factor Receptor Superfamily, Member 10c, Decoy Without An , Intracellular Domain, TRAILR3, DCR1, TRID, TNF-Related Apoptosis-Inducing Ligand Receptor, Antagonist Decoy Receptor For TRAIL/Apo-2L, Decoy TRAIL Receptor Without Death Domain, Lymphocyte Inhibitor Of TRAIL, Decoy Receptor,TRAIL-R, LIT,Tumor Necrosis Factor Receptor Superfamily Member 10C, TRAIL Receptor Without an Intracellular Domain, Cytotoxic TRAIL Receptor, TRAIL Receptor, CD263 Antigen, DCR1-TNFR, CD263.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSATTARQE EVPQQTVAPQ QQRHSFKGEE CPAGSHRSEH TGACNPCTEG VDYTNASNNE PSCFPCTVCK SDQKHKSSCT MTRDTVCQCK EGTFRNENSP EMCRKCSRCP SGEVQVSNCT SWDDIQCVEE FGANATVETP AAEETMNTSP GTPAPAAEET MNTSPGTPAP AAEETMTTSP GTPAPAAEET MTTSPGTPAP AAEETMTTSP GTPA.
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 :
RLN3 HumanDescription:
Relaxin-3 Human Recombinant
Relaxin 3, Prorelaxin H3, RXN3, Insl7, ZINS4, H3, Relaxin 3 (H3), Relaxin-3, RLN3.
Product # :
PRO-2176Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Relaxin-3 Human Recombinant produced in E.Coli is a disulfide-linked heterodimeric, non-glycosylated, polypeptide chain containing 24 amino acids for A chain and 27 amino acids for B chain and having a molecular mass of 2.5kDa for A chain and 3kDa for B chain.The Relaxin-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered solution in Acetonitrile and TFA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured by cAMP accumulation in human THP-1 cells, is less than 17.5ng/ml.More Info
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Introduction
Relaxin-3 (RLN3) belongs to the relaxin family. Relaxins are endocrine and autocrine/paracrine hormones. Relaxin, which is produced by the ovary, targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. Unlike human Relaxins 1 and 2, Relaxin 3 does not seem to have a role in reproduction; however it is involved in stress response in the brain stem. RLN3 is the only known ligand for the G-protein-coupled receptor GPCR135, titled RXFP3. In addition, RLN3 binds the LGR7 (RXFP1) receptor, however with lower affinity than Relaxin-2. Even though binding of RLN3 to LGR7 increases intracellular cAMP, binding to GPCR135 suppresses cAMP accumulation, indicating coupling to Gi, Go, or Gz by this receptor.
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Synonyms
Relaxin 3, Prorelaxin H3, RXN3, Insl7, ZINS4, H3, Relaxin 3 (H3), Relaxin-3, RLN3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized RLN3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Relaxin-3 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 RLN3 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
A chain: DVLAGLSSSC CKWGCSKSEI SSLC.
B chain: RAAPYGVRLCG REFIRAVIFT CGGSRW.
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 :
NUCB2 HumanDescription:
Nucleobindin-2 Human Recombinant
Nucleobindin-2, DNA-binding protein NEFA, Gastric cancer antigen Zg4, NUCB2, NEFA, Nesfatin.
Product # :
PRO-492Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Recombinant Human NUCB2 (Nesfatin) produced in E.coli has a molecular mass of 9.7kDa containing 82 amino acid residues of the human NUCB2.
Source
Escherichia Coli.
Formulation
The NUCB2 protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Nucleobindin-2 (also known as NUCB2 or Nesfatin) is a EF-hand calcium-binding protein. Nucleobindin-2 takes part in calcium homeostasis and is a multifunctional protein that interacts with Ca(2+) nucleic acids & various regulatory proteins in different signaling pathways. NUCB2 (Nesfatin) is localized in neuronal perikarya and dendrites of mouse brain.
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Synonyms
Nucleobindin-2, DNA-binding protein NEFA, Gastric cancer antigen Zg4, NUCB2, NEFA, Nesfatin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized NUCB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NUCB2 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 NUCB2 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
VPIDIDKTKV QNIHPVESAK IEPPDTGLYY DEYLKQVIDV LETDKHFREK LQKADIEEIK SGRLSKELDL VSHHVRTKLD 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.
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Name :
Follistatin HumanDescription:
Follistatin Human Recombinant
FST, FS
Product # :
CYT-232Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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Description
Follistatin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 288 amino acids and having a total molecular mass of 31.5kDa.The FST is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing no additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.
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Introduction
Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin functions as an ACTV antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).
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Synonyms
FST, FS
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Follistatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FST 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 Follistatin 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 Gly-Asn-Cys-Trp-Leu.
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Background
What is the molecular weight/Mw of FOLLISTATIN HUMAN Protein?
FOLLISTATIN HUMAN Protein has a total Mw of 31.5kDa.
What is the source or expression system of FOLLISTATIN HUMAN Protein?
Escherichia Coli.
What is the Purity of FOLLISTATIN HUMAN Protein?
FOLLISTATIN HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FOLLISTATIN HUMAN Protein?
The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.
What is the amino acid sequence of FOLLISTATIN HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Asn-Cys-Trp-Leu.
What applications can FOLLISTATIN HUMAN Protein be used in?
FOLLISTATIN HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FOLLISTATIN HUMAN Protein?
The endotoxin level is minimal, FOLLISTATIN 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 :
CST7 HumanDescription:
Cystatin 7 Human Recombinant
Cystatin-F, Cystatin-7, Cystatin-like metastasis-associated protein, CMAP, Leukocystatin, Cystatin 7, CST7, CMAP.
Product # :
PRO-2222Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
CST7 Human Recombinant produced in E. coli is a single polypeptide chain containing 132 amino acids (20-145) and having a molecular mass of 15.3kDa.CST7 is fused to a 7 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CST7 solution (0.5mg/1ml) contains phosphate buffered saline (pH7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Cystatin 7 (CST7) is a glycosylated cysteine protease inhibitor with a putative role in immune regulation through inhibition of a unique target in the hematopoietic system. Cystatin-7 is comprised of multiple cystatin-like sequences. The superfamily is comprised of 3 inhibitory families: the type 1 cystatins (stefins), type 2 cystatins and the kininogens. Some members are active cysteine protease inhibitors, while others have lost or possibly never had this inhibitory activity. Type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in various human fluids and secretions. CST7 protein expression has been observed in numerous human cancer cell lines established from malignant tumors.
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Synonyms
Cystatin-F, Cystatin-7, Cystatin-like metastasis-associated protein, CMAP, Leukocystatin, Cystatin 7, CST7, CMAP.
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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
GPSPDTCSQD LNSRVKPGFP KTIKTNDPGV LQAARYSVEK FNNCTNDMFL FKESRITRAL VQIVKGLKYM LEVEIGRTTC KKNQHLRLDD CDFQTNHTLK QTLSCYSEVW VVPWLQHFEV PVLRCHHHHH HH.
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 :
S100A8 Human, HisDescription:
S100 Calcium Binding Protein A8 Human Recombinant, His Tag
Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.
Product # :
PRO-150Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
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Description
The Recombinant Human S100A8 produced in E.coli has a molecular mass of 12.08kDa containing 103 amino acid residues of the human S100A8 and fused to a 10 a.a. His tag at N-terminus.
Source
Escherichia Coli.
Formulation
S100A8 was filtered (0.4µm) and lyophilized in 0.5mg/ml in 20mM Tris and 100mM NaCl, pH 7.5.
More Info
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Introduction
S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.
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Synonyms
Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS MLTELEKALN SIIDVYHKYS LIKGNFHAVY RDDLKKLLET ECPQYIRKKG ADVWFKELDI NTDGAVNFQEMLTELEKALN SIIDVYHKYS LIKGNFHAVY RDDLKKLLET ECPQYIRKKG ADVWFKELDI NTDGAVNFQE FLILVIKMGV AAHKKSHEES HKE.
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 :
AHSG MouseDescription:
Alpha-2-HS-Glycoprotein Mouse Recombinant
Alpha-2-HS-glycoprotein, Countertrypin, Fetuin-A.
Product # :
PRO-2220Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
AHSG produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 333 amino acids (19-345.a.) and having a molecular mass of 36.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). AHSG is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
AHSG protein solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
AHSG (fetuin-A) which is a glycoprotein present in the serum, is synthesized by hepatocytes. AHSG is one of the fetuin class of plasma binding proteins. It is involved in a number of functions, such as endocytosis, brain development and the formation of bone tissue. It is usually present in the cortical plate of the immature cerebral cortex and bone marrow hemopoietic matrix, hence it has been postulated that it participates in the development of the tissues. Yet, its exact significance is still vague. AHSG promotes endocytosis, hold opsonic properties and influences the mineral phase of the bone. Affinity for calcium and barium ions has been shown.
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Synonyms
Alpha-2-HS-glycoprotein, Countertrypin, Fetuin-A.
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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
APQGTGLGFR ELACDDPEAE QVALLAVDYL NNHLLQGFKQ VLNQIDKVKV WSRRPFGVVY EMEVDTLETT CHALDPTPLA NCSVRQLTEH AVEGDCDFHI LKQDGQFRVM HTQCHSTPDS AEDVRKLCPR CPLLTPFNDT NVVHTVNTAL AAFNTQNNGT YFKLVEISRA QNVPLPVSTL VEFVIAATDC TAKEVTDPAK CNLLAEKQHG FCKANLMHNL GGEEVSVACK LFQTQPQPAN ANAVGPVPTA NAALPADPPA SVVVGPVVVP RGLSDHRTYH DLRHAFSPVA SVESASGETL HSPKVGQPGA AGPVSPMCPG RIRHFKIHHH 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.