Search results
1000 results found for “insulin”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
Der F1Description:
Der F1 Mosaic Protein Recombinant
Product # :
ALR-004Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
The E.Coli derived recombinant protein contains the Dermatophagoides farina Der F1 full length protein (a.a. 1-320) and fused to a 6 His Tag at C-terminus, having a total Mw of 36kDa, pI 5.88.
Source
E.Coli.
Formulation
60mM NaCl, 50mM Tris-HCl pH 8.0 and 1.2M Urea.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining) and RP-HPLC.
More Info
-
Introduction
DERF1 is a thiol protease that hydrolyzes proteins, with a preference for Phe or basic residues. DERF1 is a C1 peptidase family member. DERF1 has extensive endopeptidase specificity. DERF1 causes an allergic reaction in humans. Common symptoms of mite allergy are bronchial asthma, allergic rhinitis and conjunctivitis.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Der F1 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Purification Method
Purified by proprietary chromatographic technique.
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 :
Activin-A Human Plant-ActiveDescription:
Activin-A Human Recombinant, Plant-Active
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-414Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Active form Activin-A Human Recombinant produced in Plant is a homodimeric, glycosylated, polypeptide chain containing 2 x 116 amino acids and having a molecular weight of 27.4kDa.The Active form Activin-A is fused to a 6-His tag at N-terminus and purified by standard chromatographic techniques.
Source
Nicotiana benthamiana.
Formulation
Active form Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 50mM Tris-HCl pH-7.4
Purity
Greater than 98% as obsereved by SDS-PAGE.
Biological Activity
The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.More Info
-
Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
-
Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
-
Physical Appearance
Lyophilized freeze dried powder.
-
Stability
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Repeated freezing and thawing is not recommended.
-
Solubility
INHBA protein should be reconstituted in distilled water to a concentration of 50 ug /ml. Due to the protein nature, dimmers and multimers may be observed.
-
Amino Acid Sequence
HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSG
YHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFA
NLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS. -
Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 27.4 kDa.What is the source or expression system of Activin A Protein?
Nicotiana benthamiana.What is the Purity of Activin A Protein?
Activin A Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin A Protein?
The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.What is the endotoxin level for Activin A Protein?
The endotoxin level is minimal, ACTIVIN A Protein was purified using conventional chromatography techniques.What is the amino acid sequence of ACTIVIN A Protein?HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS
What applications can ACTIVIN-A Protein be used in?
ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CPA4 HumanDescription:
Carboxypeptidase A4 Human Recombinant
Carboxypeptidase A4, Carboxypeptidase A3, CPA3, EC 3.4.17.1, EC 3.4.17.-, EC 3.4.17, Carboxypeptidase A4, Carboxypeptidase A3.
Product # :
ENZ-942Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CPA4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 413 amino acids (17-421a.a.) and having a molecular mass of 46.6kDa.CPA4 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CPA4 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Carboxypeptidase A4 (CPA4) belongs to the carboxypeptidase A/B subfamily, and it is located in a cluster with 3 other family members on chromosome 7. CPA4 is a secreted, zinc-dependent metallocarboxypeptidase, which removes the C-terminal amino acid from peptides having a free C-terminal carboxyl group. CPA4 is a metalloprotease which may be involved in the histone hyperacetylation pathway. CPA4 are synthesized as zymogens which are activated by proteolytic cleavage.
-
Synonyms
Carboxypeptidase A4, Carboxypeptidase A3, CPA3, EC 3.4.17.1, EC 3.4.17.-, EC 3.4.17, Carboxypeptidase A4, Carboxypeptidase A3.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
GQEKFFGDQV LRINVRNGDE ISKLSQLVNS NNLKLNFWKS PSSFNRPVDV LVPSVSLQAF KSFLRSQGLE YAVTIEDLQA LLDNEDDEMQ HNEGQERSSN NFNYGAYHSL EAIYHEMDNI AADFPDLARR VKIGHSFENR PMYVLKFSTG KGVRRPAVWL NAGIHSREWI SQATAIWTAR KIVSDYQRDP AITSILEKMD IFLLPVANPD GYVYTQTQNR LWRKTRSRNP GSSCIGADPN RNWNASFAGK GASDNPCSEV YHGPHANSEV EVKSVVDFIQ KHGNFKGFID LHSYSQLLMY PYGYSVKKAP DAEELDKVAR LAAKALASVS GTEYQVGPTC TTVYPASGSS IDWAYDNGIK FAFTFELRDT GTYGFLLPAN QIIPTAEETW LGLKTIMEHV RDNLYLEHHH 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.
- View Data Sheet
Name :
NCL HumanDescription:
Nucleolin Human Recombinant
Nucleolin, Protein C23, NCL, C23.
Product # :
PRO-1508Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Nucleolin Human Recombinant produced in SF9 is a glycosylated, polypeptide chain containing the C-terminal section of the human nucleolin and missing the N-terminal histone-binding part of nucleolin, having a calculated molecular mass of 55,162 Dalton. NCL is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 Insect Cells.
Formulation
NCL is supplied in 20mM HEPES pH-7.3, 600mM NaCl, 0.3mM Tris(2-carboxyethyl)phosphine (TCEP) and 25% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
-
Introduction
Nucleolin (NCL) which is a eukaryotic nucleolar phosphoprotein, involved in the synthesis and maturation of ribosomes. Nucleolin is the key nucleolar protein of growing eukaryotic cells. NCL is found linked with intranucleolar chromatin and pre-ribosomal particles. NCL induces chromatin decondensation by binding to histone H1. Nucleolin is assumed to have a role in pre-rRNA transcription and ribosome compilation. Nucleolin may also have a role in the process of transcriptional elongation. Nucleolin is located primarily in the dense fibrillar regions of the nucleolus. The Human NCL gene consists of 14 exons with 13 introns and spans approximately 11kb.
-
Synonyms
Nucleolin, Protein C23, NCL, C23.
-
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. 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.
- View Data Sheet
Name :
IL 8 AntibodyDescription:
Interleukin-8, Mouse Anti-Human
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
Product # :
ANT-111Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- formulation
- More Info
Formulation
1mg/ml in PBS (after reconstitution).
More Info
-
Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies.
When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytosethe particle. Upon processing, they release chemokinesto signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophilsat the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor. -
Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
-
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
-
Immunogen
r.Human IL-8.
-
Ig Subclass
Mouse IgG1.
-
Clone
NYR-HIL8.
-
Applications
Direct ELISA, Western Blot, Immuneprecipitation, Immunohistochemistry.
-
Cross reactivity
No cross reactivity with murine IL-8 was detected.
-
Note
This antibody was produced in BALB/c mice.
-
Titer
By direct ELISA, 1:20,000 dilution will yield >1.0 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
-
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
-
Type
Mouse Anti Human Monoclonal.
-
Storage Procedures
In lyophilized form, for long periods, store at 4C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20C.
-
Purification Method
Ion exchange.
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 :
CRH HumanDescription:
Corticotropin Releasing Hormone Human Recombinant
CRF, Corticotropin-Releasing Factor.
Product # :
HOR-053Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
The CRH Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The CRH His-Tagged Fusion Protein, produced in E. coli, is a 21kDa protein containing 154 amino acid residues of the CRH Human, 43-196 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Synonyms
CRF, Corticotropin-Releasing Factor.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized CRH 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.
-
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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
-
Background
Corticotropin-Releasing Hormone (CRH) is a neuropeptide which regulates the body's response to stress. CRH stimulates the release of ACTH from the pituitary gland which triggers the adrenal glands to produce cortisol. CRH takes part in the hypothalamic-pituitary-adrenal axis which controls the production of cortisol and more various glucocorticoids. CRH is synthesized in different tissues such as the brainstem, hypothalamus and peripheral organs.
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 :
IL 10 Human, HisDescription:
Interleukin-10 Human Recombinant, His
B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.
Product # :
CYT-486Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Interleukin-10 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 181 amino acids fragment (19-178) and having a total molecular mass of 20.94kDa with a 20 amino acids N-Terminal His tag. The IL-10 His-Tag protein is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Interleukin-10 His is supplied in 20mM Tris-HCl pH-8 and 20% glycerol.
Purity
Greater than 95.0% by SDS-PAGE.
More Info
-
Introduction
Interleukin-10 is a multifunctional cytokine produced by a variety of cell types including T helper cells activated B cells and activated macrophages. Interleukin-10 regulates immune-mediated inflammation and modulates the function of cells such as lymphocytes, monocytes, natural killer cells and dendritic cells.
-
Synonyms
B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.
-
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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSPGQGTQSE NSCTHFPGNL PNMLRDLRDA FSRVKTFFQM KDQLDNLLLK ESLLEDFKGY LGCQALSEMI QFYLEEVMPQ AENQDPDIKA HVNSLGENLK TLRLRLRRCH RFLPCENKSK AVEQVKNAFN KLQEKGIYKA MSEFDIFINY IEAYMTMKIR 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 :
IL 1RA RatDescription:
Interleukin-1 Receptor Antagonist Rat Recombinant
IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.
Product # :
CYT-152Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
IL 1RA Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 152 amino acids and having a molecular mass of 17.5kDa.The IL 1RA Rat is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Fully biologically active when compared to standard. Measured by its ability to inhibit IL1a-dependent proliferation in D10.G4.1 mouse helper T cells. The ED50 for this effect is typically 30-150ng/ml (corresponding to a specific activity of 6,667-33,334units/mg ) in the presence of 50pg/ml of rrIL1a.More Info
-
Introduction
Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.
-
Synonyms
IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized IL 1RA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL 1RA should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized IL 1RA in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
HPAGKRPCKM QAFRIWDTNQ KTFYLRNNQL IAGYLQGPNT KLEEKIDMVP IDFRNVFLGI HGGKLCLSCV KSGDDTKLQL EEVNITDLNK NKEEDKRFTF IRSETGPTTS FESLACPGWF LCTTLEADHP VSLTNTPKEP CTVTKFYFQE DQ
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 :
Influenza-A Solomon IslandsDescription:
H1N1 Influenza-A Virus Solomon Islands/03/06
Product # :
IHA-022Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- formulation
- purity
- More Info
Description
Allantoic fluid of 10 days old embryonated eggs, inoculated with influenza A virus, strain A/Solomon Islands/03/06. The Influenza Virus was purified by Ultracentrifugation with 10-40 % sucrose gradient.
Formulation
The H1N1 A/Solomon Islands/03/06 solution contains 0.1M NaCl, 10mM Tris-HCl, 1mM EDTA pH-8 (STE), 0.1% sodium azide (NaN3) and 0.005% thimerosal.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
H1N1 is a subtype specie of Influenza A virus. H1N1 Influenza Virus has mutated into various strains such as the Spanish Flu strain, mild human flu strains, endemic pig strains, and various strains found in birds.
The Influenza A Virus is a globular particle about 100nm in diameter, sheathed in a lipid bilayer derived from the plasma membrane of its host. Studded in the lipid bilayer are two integral membrane proteins some 500 molecules of hemagglutinin ("H") and some 100 molecules of neuraminidase ("N"). Within the lipid bilayer are 3000 molecules of matrix protein and 8 pieces of RNA. Each of the 8 RNA molecules is associated with many copies of a nucleoprotein, several molecules of the three subunits of its RNA polymerase some "non-structural" protein molecules of uncertain function. -
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
A/Solomon Islands/03/06 although stable 4°C for 4 weeks, should be stored below -18°C. Please prevent freeze-thaw cycles.
-
Inactivation
Thimerosal and beta propiolactone treatment.This product has been treated in a manner consistent with methods of inactivation. Generally accepted good laboratory practices appropriate to microbiological/viral safe handling practices and techniques are required at work.
-
Immunological Activity
Tested with anti-influenza A monoclonal antibodies in ELISA.Serological studies of influenza A virus, immunogen for antibody production.
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 :
HSA ProteinDescription:
HSA Human Protein
HSA, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.
Product # :
PRO-354Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
HSA contains 584 amino acid residues derived from the prototypicalHSA sequence.
Source
Human Serum.
Formulation
0.2gr/ml solution containing no additives.
Purity
Greater than 97.0% as determined by SDS-PAGE.
More Info
-
Introduction
HSA is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted HSA. HSA is a soluble, monomeric protein which comprises about one-half of the blood serum protein. HSA functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. HSA is a globular unglycosylated serum protein of molecular weight 65,000. The human HSA gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
HSA is widely used to stabilize blood volume generally from donors but the fear of contamination such as HIV & Hepatitis has enticed great interest in the recombinant form which is identical to the natural blood.
Suitable for use in biochemical, excipient (an inert substance used as a diluent or vehicle for a drug), culture media and chromatographic applications. -
Synonyms
HSA, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.
-
Physical Appearance
Sterile Filtered clear yellowish solution.
-
Stability
HSA although stable at room temperature for 2 weeks should be stored at 4°C.
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 :
ATF BovineDescription:
Apo Transferrin Bovine
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.
Product # :
PRO-511Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Bovine Apo Transferrin is a glycoprotein of approximately 77kDa.
Source
Bovine Serum.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
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.
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 are Molecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells. -
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.
-
Physical Appearance
Sterile Filtered off-white lyophilized (freeze-dried) powder.
-
Stability
Store the lyophilized Apo Transferrin between 2-8°C, do not freeze.
-
Solubility
It is recommended to reconstitute the lyophilized Apo Transferrin in sterile 18MΩ-cm H2O not less than 1gr/30ml in 20min. at 20-25C.
-
Iron Content
The Iron content was estimated by ICP-OES and was found to be less than 40 ppm.
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 :
AngiotensinDescription:
Angiotensin
Angiotensinogen, Serpin A8, ANHU, SERPINA8.
Product # :
ENZ-283Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- purity
- More Info
Description
Angiotensin contains a total of 8 amino acids having a molecular weight of 1031.2 Dalton and a molecular formula of C49H70N14O11.
Source
Synthetic.
Purity
Greater than 98.0% as determined by RP-HPLC.
More Info
-
Introduction
Angiotensin is an oligopeptide in the blood that causes vasoconstriction, increased blood pressure, and release of aldosterone from the adrenal cortex. It is a powerful dipsogen. It is derived from the precursor molecule angiotensinogen, a serum globulin produced in the liver. It plays an important role in the renin-angiotensin system.
The protein encoded by this gene, pre-angiotensinogen or angiotensinogen precursor, is expressed in the liver and is cleaved by the enzyme renin in response to lowered blood pressure. The resulting product, angiotensin I is then cleaved by angiotensin converting enzyme (ACE) to generate the physiologically active enzyme angiotensin II. The protein is involved in maintaining blood pressure and in the pathogenesis of essential hypertension and preeclampsia. -
Synonyms
Angiotensinogen, Serpin A8, ANHU, SERPINA8.
-
Physical Appearance
Sterile Filtered white lyophilized powder.
-
Stability
Lyophilized Angiotensin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Serpin A8 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Angiotensin in sterile 18MΩ-cm H2O not less than 100 µg/ml or more than 10 mg/ml solutions.
-
Amino Acid Sequence
Asn-Arg-Val-Tyr-Val-His-Pro-Phe-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 :
DCN MouseDescription:
Decorin Mouse Recombinant
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN.
Product # :
PRO-2234Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
DCN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (17-354 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 344 amino acids and having a molecular mass of 38.8kDa.DCN shows multiple bands between 40-57kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
DCN protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 30% glycerol and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.
-
Synonyms
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
GPFEQRGLFD FMLEDEASGI IPYDPDNPLI SMCPYRCQCH LRVVQCSDLG LDKVPWDFPP DTTLLDLQNN KITEIKEGAF KNLKDLHTLI LVNNKISKIS PEAFKPLVKL ERLYLSKNQL KELPEKMPRT LQELRVHENE ITKLRKSDFN GLNNVLVIEL GGNPLKNSGI ENGAFQGLKS LSYIRISDTN ITAIPQGLPT SLTEVHLDGN KITKVDAPSL KGLINLSKLG LSFNSITVME NGSLANVPHL RELHLDNNKL LRVPAGLAQH KYIQVVYLHN NNISAVGQND FCRAGHPSRK ASYSAVSLYG NPVRYWEIFP NTFRCVYVRS AIQLGNYKHH HHHH
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 :
IL 1 beta Human, HEKDescription:
Interleukin-1 beta Human Recombinant, HEK
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
Product # :
CYT-094Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Interleukin-1 beta Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 18-25kDa due to glycosylation.The IL-1 beta is purified by proprietary chromatographic techniques.
Source
HEK.
Formulation
The IL-1 beta was lyophilized from 1mg/ml in 1xPBS.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
The specific activity was determined by the dose-dependent stimulation of the proliferation of mouse D10S cells and is typically 0.02-0.08ng/ml.More Info
-
Introduction
Interleukin-1b is produced by activated macrophages, IL-1B stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.
-
Synonyms
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized IL-1 beta although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1 beta should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized IL-1b in sterile PBS containing 0.1% endotoxin-free recombinant HSA.
-
Amino Acid Sequence
APVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFVQGEESNDKIP
VALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKMEKRFVFNKIEINNKLEFES
AQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS.
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 :
PFN2 HumanDescription:
Profilin-2 Human Recombinant
Profilin-II, PFN2, Profilin-2, PFL, D3S1319E.
Product # :
PRO-809Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
PFN2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids (1-140 a.a.) and having a molecular mass of 17.2 kDa. PFN2 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
PFN2 protein solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
PFN2 is a ubiquitous actin monomer-binding protein which is part of the profilin family. PFN2 regulates actin polymerization in response to extra cellular signals. PFN2 binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, while it increases it at low concentrations. PFN2 binds to PIP2, it inhibits the formation of IP3 and DG.
-
Synonyms
Profilin-II, PFN2, Profilin-2, PFL, D3S1319E.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAGWQSYVDN LMCDGCCQEA AIVGYCDAKY VWAATAGGVF QSITPIEIDM IVGKDREGFF TNGLALGAKK CSVIRDSLYV DGDCTMDIRT KSQGGEPTYN VAVGRAGRVL VFVMGKEGVH GGGLNKKAYS MAKYLRDSGF.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
MED7 HumanDescription:
Mediator Complex Subunit 7 Human Recombinant
Mediator complex subunit 7, cofactor required for Sp1 transcriptional activation subunit 9 33kDa, Activator-recruited cofactor 34 kDa component, Transcriptional coactivator CRSP33, RNA polymerase transcriptional regulation mediator subunit 7 homolog, mediator of RNA polymerase II transcription subunit 7, CRSP complex subunit 9, CRSP33, CRSP9, ARC34, hMED7.
Product # :
PRO-1319Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
MED7 Human Recombinant produced in E. coli is a single polypeptide chain containing 256 amino acids (1-233) and having a molecular mass of 29.7 kDa.MED7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The MED7 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
MED7 is a member of the Mediator complex subunit 7 family. The activation of gene transcription is a multistep course which is initiated by factors which identify transcriptional enhancer sites in DNA and collaborate with co-activators to direct transcriptional initiation by the RNA polymerase II apparatus. The gene encode a subunit of the CRSP (cofactor required for SP1 activation) complex, that, together with TFIID, is needed for effective activation by SP1. Additionally, MED7 is also an element of other multisubunit complexes e.g. thyroid hormone receptor-(TR-) associated proteins that cooperate with TR and enables TR function on DNA templates in conjunction with initiation factors and cofactors.
-
Synonyms
Mediator complex subunit 7, cofactor required for Sp1 transcriptional activation subunit 9 33kDa, Activator-recruited cofactor 34 kDa component, Transcriptional coactivator CRSP33, RNA polymerase transcriptional regulation mediator subunit 7 homolog, mediator of RNA polymerase II transcription subunit 7, CRSP complex subunit 9, CRSP33, CRSP9, ARC34, hMED7.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMGEPQQV SALPPPPMQY IKEYTDENIQ EGLAPKPPPP IKDSYMMFGN QFQCDDLIIR PLESQGIERL HPMQFDHKKE LRKLNMSILI NFLDLLDILI RSPGSIKREE KLEDLKLLFV HVHHLINEYR PHQARETLRV MMEVQKRQRL ETAERFQKHL ERVIEMIQNC LASLPDDLPH SEAGMRVKTE PMDADDSNNC TGQNEHQREN SGHRRDQIIE KDAALCVLID EMNERP
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 :
S100A4 HumanDescription:
S100 Calcium-Binding Protein A4 Human Recombinant
Protein S100-A4, S100 calcium-binding protein A4, Metastasin, Protein Mts1, Placental calcium-binding protein, Calvasculin, S100A4, CAPL, MTS1, 42A, 18A2, FSP1, P9KA, PEL98.
Product # :
PRO-698Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
S100A4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 121 amino acids (1-101) and having a molecular mass of 13.8 kDa.The S100A4 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
S100A4 protein at in 20mM Tris-HCl, pH-8 & 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
S100A4 is part of the S100 super-family of proteins containing 2 EF-hand calcium binding domains. S100A4 is ubiquitously overexpressed and is localized in the cytoplasm and/or nucleus. S100A4 is involved in motility, invasion, and tubulin polymerization. Chromosomal rearrangements and altered expression of the S100A4 gene have been implicated in tumor metastasis.
-
Synonyms
Protein S100-A4, S100 calcium-binding protein A4, Metastasin, Protein Mts1, Placental calcium-binding protein, Calvasculin, S100A4, CAPL, MTS1, 42A, 18A2, FSP1, P9KA, PEL98.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MACPLEKALD VMVSTFHKYS GKEGDKFKLN KSELKELLTR ELPSFLGKRT DEAAFQKLMS NLDSNRDNEVDFQEYCVFLS CIAMMCNEFF EGFPDKQPRK 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.
- View Data Sheet
Name :
Actin RabbitDescription:
Actin Rabbit
Product # :
PRO-517Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Ultra pure Actin consists in the alpha-skeletal muscle isoform and is purified from rabbit striated muscle.The purification method used (according to Spudich & Watts) results in a highly purified protein having a Molecular mass of 43,000 dalton.
Source
Rabbit Muscle.
Formulation
The protein was lyophilized from a 1mg/ml solution containing 10mM Tris/HCl buffer pH 8.0, 0.2mM CaCl2, 0.2mM ATP, 1mM DTT and 0.5% (w/v) SDS.
Purity
Greater than 98.0% as determined by SDS-PAGE.
More Info
-
Introduction
Actin is a muscle protein localized in the I band of the myofibrils; acting along with myosin, it is responsible for contraction and relaxation of muscle. Each actin protomer binds one molecule of ATP and has one high affinity site for either calcium or magnesium ions, as well as several low affinity sites. Actin exists as a monomer in low salt concentrations, but filaments form rapidly as salt concentration rises, with the consequent hydrolysis of ATP. It occurs in globular (G-actin) and fibrous (F-actin) forms. Actin is found in all eukaryotic cells (except for nematode sperm). Actin is one of the most highly-conserved proteins, differing by no more than 20% in species as diverse as algae and humans. Its other functions include cell motility, cell division and cytokinesis, vesicle and organelle movement, cell signaling, and the establishment and maintenance of cell junctions and cell shape.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store the Lyophilized Actin between 2-8°C, do not freeze. Upon reconstitution Actin should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Actin in sterile 18MΩ-cm H2O not less than 1mg/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 :
AITRL Human, HisDescription:
AITRL Human Recombinant, His Tag
Osteostat, TNFSF18, Activation-induced TNFR member Ligand, GITRL,TL6, AITRL, Glucocorticoid-induced TNF-related ligand, hGITRL, Tumor necrosis factor ligand superfamily member 18, MGC138237.
Product # :
CYT-317Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
AITRL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain (aa 50-177) containing a total of 137 amino acids and having a molecular mass of 15.6kDa. The AITRL protein is fused to a 9 aa His Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AITRL protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0) & 10% glycerol.
Purity
Greater than 85.0% as determined bySDS-PAGE.
More Info
-
Introduction
Osteostat is the cytokine that binds to TNFRSF18/AITR/GITR and is important for interactions between activated T-lymphocytes and endothelial cells and may modulate T-lymphocyte survival in peripheral tissues. Osteostat is expressed at high levels in the small intestine, ovary, testis, kidney and endothelial cells after stimulation by lipopolysaccharides.
Osteostat protein is detectable in human microvascular EC and is highly up-regulated by IFN-alpha and IFN-beta. Osteostat inhibit differentiation of osteoclasts from monocytic precursor cells. Osteostat suppresses the early stage of osteoclastogenesis via inhibition of macrophage colony-stimulating factorinduced receptor activator of NF-kappaB (RANK) expression in the osteoclast precursor cells. Osteostat does not inhibit lipopolysaccharide-induced RANK expression in monocytes and dendritic cells, or activation-induced RANK expression in T cells. Osteostat is a novel regulator of osteoclast generation and substantiate the major role played by the endothelium in bone physiology. -
Synonyms
Osteostat, TNFSF18, Activation-induced TNFR member Ligand, GITRL,TL6, AITRL, Glucocorticoid-induced TNF-related ligand, hGITRL, Tumor necrosis factor ligand superfamily member 18, MGC138237.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MQLETAKEPC MAKFGPLPSK WQMASSEPPC VNKVSDWKLE ILQNGLYLIY GQVAPNANYN DVAPFEVRLY KNKDMIQTLT NKSKIQNVGG TYELHVGDTI DLIFNSEHQV LKNNTYWGII LIANPQEISL EHHHHHH.
-
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 15.6kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What is the amino acid sequence of ADIPONECTIN Protein?
MQLETAKEPC MAKFGPLPSK WQMASSEPPC VNKVSDWKLE ILQNGLYLIY GQVAPNANYN DVAPFEVRLY KNKDMIQTLT NKSKIQNVGG TYELHVGDTI DLIFNSEHQV LKNNTYWGII LIANPQEISL EHHHHHH
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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 :
SENP8 HumanDescription:
Sentrin Specific Peptidase Family Member 8 Human Recombinant
SUMO/sentrin specific peptidase family member 8, DEN1, NEDP1, Protease cysteine 2 (NEDD8 specific), PRSC2, NEDD8-specific protease 1, HsT17512, Deneddylase-1, NEDD8 specific-protease cysteine 2, Sentrin/SUMO-specific protease SENP8.
Product # :
ENZ-146Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SENP8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-212) and having a molecular mass of 26.2 kDa.The SENP8 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SENP8 protein 1mg/ml is supplied in 20mM Tris-HCL, pH-8, 0.1M NaCl, 1mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
SENP8 is a cysteine protease which belongs to the sentrin-specific protease family. SENP8 takes part in processing and deconjugation of the ubiquitin-like protein labeled, neural precursor cell expressed developmentally downregulated 8(NEDD8).
-
Synonyms
SUMO/sentrin specific peptidase family member 8, DEN1, NEDP1, Protease cysteine 2
(NEDD8 specific), PRSC2, NEDD8-specific protease 1, HsT17512, Deneddylase-1, NEDD8 specific-protease cysteine 2, Sentrin/SUMO-specific protease SENP8. -
Physical Appearance
SENP8 is supplied as a sterile filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDPVVLSYMD SLLRQSDVSL LDPPSWLNDH IIGFAFEYFA NSQFHDCSDH VSFISPEVTQ FIKCTSNPAE IAMFLEPLDL PNKRVVFLAI NDNSNQAAGG THWSLLVYLQ DKNSFFHYDS HSRSNSVHAK QVAEKLEAFL GRKGDKLAFV EEKAPAQQNS YDCGMYVICN TEALCQNFFR QQTESLLQLL TPAYITKKRG EWKDLITTLA KK
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 :
I TAC Human, HisDescription:
I-TAC Human Recombinant (CXCL11), His Tag
Small inducible cytokine B11, CXCL11, Interferon-inducible T-cell alpha chemoattractant, I-TAC, Interferon-gamma-inducible protein 9, IP-9, H174, Beta-R1, chemokine (C-X-C motif) ligand 11, IP9, b-R1, SCYB11, SCYB9B, MGC102770.
Product # :
CHM-232Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
I-TAC (CXCL11) Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 94 amino acids (22-94) and having a molecular mass of 10.6kDa.I-TAC is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The I-TAC solution (1mg/ml) contains 10mM sodium citrate(pH 3.5), 20% glycerol and 2mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Chemokine (C-X-C motif) ligand 11 (CXCL11) is a small cytokine belonging to the CXC chemokine family that is also called Interferon-inducible T-cell alpha chemoattractant (I-TAC) and Interferon-gamma-inducible protein 9 (IP-9). It is highly expressed in peripheral blood leukocytes, pancreas and liver, with moderate levels in thymus, spleen and lung and low expression levels were in small intestine, placenta and prostate. Gene expression of CXCL11 is strongly induced by IFN-g and IFN-b, and weakly induced by IFN-a. This chemokine elicits its effects on its target cells by interacting with the cell surface chemokine receptor CXCR3, with a higher affinity than do the other ligands for this receptor, CXCL9 and CXCL10. CXCL11 is chemotactic for activated T cells. Its gene is located on human chromosome 4 along with many other members of the CXC chemokine family.
-
Synonyms
Small inducible cytokine B11, CXCL11, Interferon-inducible T-cell alpha chemoattractant, I-TAC, Interferon-gamma-inducible protein 9, IP-9, H174, Beta-R1, chemokine (C-X-C motif) ligand 11, IP9, b-R1, SCYB11, SCYB9B, MGC102770.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MFPMFKRGRC LCIGPGVKAV KVADIEKASI MYPSNNCDKI EVIITLKENK GQRCLNPKSK QARLIIKKVE RKNF.
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 :
EFNA1 HumanDescription:
Ephrin A1 Human Recombinant
Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.
Product # :
PRO-971Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
EFNA1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 185 amino acids (19-182) and having a molecular mass of 21.6 kDa.EFNA1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The EFNA1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
EFNA1 belongs to the ephrin (EPH) family. The EPH subfamily is the biggest group of receptor protein kinases and they take part in vital nervous system function and development.
-
Synonyms
Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDRHTVFWNS SNPKFRNEDY TIHVQLNDYV DIICPHYEDH SVADAAMEQY ILYLVEHEEY QLCQPQSKDQ VRWQCNRPSA KHGPEKLSEK FQRFTPFTLG KEFKEGHSYY YISKPIHQHE DRCLRLKVTV SGKITHSPQA HVNPQEKRLA ADDPEVRVLH SIGHS
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TAC3 HumanDescription:
Tachykinin-3 Human Recombinant
Tachykinin-3, ZNEUROK1, Neurokinin-B, NKB, Neuromedin-K, TAC3, NKNB, PRO1155.
Product # :
PRO-716Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TAC3 Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids (17-121 a.a.) and having a molecular mass of 13.8kDa.The TAC3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TAC3 solution contains 20mM Tris-HCl buffer (pH 8.0) and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Tachykinin-3 belongs to the substance P-related tachykinin family. Tachykinins are active peptides that stimulate neurons, induce behavioral responses, are effective vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. TAC3 and its receptor are essential switches of regulator of human puberty, regulated by the brain through the release of the GnRH which starts a chain of processes which eventually lead to the production of sex hormones.
During pregnancy, the expression of TAC3 is restricted to the outer syncytiotrophoblast of the placenta, significant concentrations of TAC3 can be identified in plasma as early as week 9, and plasma concentrations of TAC3 are grossly elevated in pregnancy-induced hypertension and pre-eclampsia. Higher Tachykinin-3 concentrations in normotensive pregnant women may be caused by the advanced gestational age and/or the result of a negative interaction of other vasoactive substances. TAC3 has a role in the continuance of high placental blood flow in normal pregnancy. -
Synonyms
Tachykinin-3, ZNEUROK1, Neurokinin-B, NKB, Neuromedin-K, TAC3, NKNB, PRO1155.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH QSFGAVCKEP QEEVVPGGGR SKRDPDLYQL LQRLFKSHSS LEGLLKALSQ ASTDPKESTS PEKRDMHDFF VGLMGKRSVQ PDSPTDVNQE NVPSFGILKY PPRAE.
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 :
TXN1 HumanDescription:
Thioredoxin Human Recombinant
Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.
Product # :
PRO-569Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Thioredoxin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 105 amino acids and having a molecular mass of 11.7 kDa.
Source
Escherichia Coli.
Formulation
Thioredoxin solution containing 1mg/ml solution containing 1xPBS pH 7.4.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is>150 A650/min/mg, obtained by measuring the increase of insulin precipitation in absorbance at 650 nm resulting from the reduction of insulin.
More Info
-
Introduction
Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation.
-
Synonyms
Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVIFLEVDVD DCQDVASECE VKCMPTFQFFKKGQKVGEFS GANKEKLEAT INELV.
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.