Search results
1000 results found for “insulin”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
Protein GDescription:
Protein G Recombinant
Product # :
PRO-402Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
- sds-page
Description
The Protein G is a single, non-glycosylated protein contains 200 amino acids having a molecular mass of 21.8kDa. The Protein-G migrates on SDS-PAGE around 32kDa.
Source
Escherichia Coli.
Formulation
Lyophilized white powder containing no additives.
Purity
>96% as determined by SDS-PAGE and RP-HPLC.
sds-page
More Info
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Recombinant Protein G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein G should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
-
Solubility
Reconstitution with deionized water or PBS.
-
Amino Acid Sequence
LPKTDTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDAT KTFTVTEKPEVIDASELTPAVTTYKLVINGKTLKGETTTEAVDAATAEKVFK QYANDNGVDGEWTYDDATKTFTVTEKPEVIDASELTPAVTTYKLVINGKTL KGETTTKAVDAETAEKAFKQYANDNGVDGVWTYDDATKTFTVTE.
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 :
PTHrP HumanDescription:
Parathyroid Hormone Related Protein Human Recombinant
Parathyroid Hormone 2, PTH2, TIPF39, Tuberoinfundibular 39 Residue Protein.
Product # :
HOR-004Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
PTHrP Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids, having an MW of 9.9kDa.The PTHrP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PthRp protein was lyophilized from a 0.2µm filtered concentrated solution in 10Mm PB, pH 6.0, 300 Mm NaCI.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
PTHrP is a powerful and discriminating agonist of PTH2R which takes part in adenyl cyclase activation and intracellular calcium levels elevation. PTHrP encourages protein kinase C beta activation, recruitment of beta-arrestin and PTH2R internalization. Additionally, PTHrP inhibits cell proliferation through its contribution to PTH2R activation, activates nociceptors and nociceptive circuits and acts as a neuropeptide in spermatogenesis.
-
Synonyms
Parathyroid Hormone 2, PTH2, TIPF39, Tuberoinfundibular 39 Residue Protein.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized PTHrP although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution PTHrP should be stored at 4C between 2-7 days and for future use below -18C.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 PTHrP in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
AVSEHQLLHD KGKSIQDLRR RFFLHHLIAE IHTAEIRATS EVSPNSKPSP NTKNHPVRFG SDDEGRYLTQ ETNKVETYKE QPLKTP.
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 :
IDH1Description:
Isocitrate Dehydrogenase-1 Yeast Recombinant
Isocitrate dehydrogenase [NADP] cytoplasmic, EC 1.1.1.42, Cytosolic NADP-isocitrate dehydrogenase, Oxalosuccinate decarboxylase, IDH, NADP(+)-specific ICDH, IDP, PICD.
Product # :
ENZ-289Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Recombinant Saccharomyces Cerevisiae ICDH (NADP) derived from yeast host cells by using over-expression system, is full length same as designated ICD1 from Saccharomyces Cerevisiae. The N-terminal amino acid Phenylalanine residue next to Met is substituted with Alanine for overexpression. The ICDH is purified by proprietary chromatographic techniques.
Source
Yeast cells.
Formulation
One ml of solution contains 0.075 mol/l KPO4, 50% Glycerol, pH 7.1.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
The specific activity was found to be 115 U/mg.More Info
-
Introduction
Isocitrate Dehydrogenase is an enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle.
-
Synonyms
Isocitrate dehydrogenase [NADP] cytoplasmic, EC 1.1.1.42, Cytosolic NADP-isocitrate dehydrogenase, Oxalosuccinate decarboxylase, IDH, NADP(+)-specific ICDH, IDP, PICD.
-
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.
-
Unit Definition
One unit is defined as 1 µmol of NAD+ production per minute under the assay conditions (25°C, pH 7.5).
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 :
RTP4 HumanDescription:
Receptor Transporter Protein 4 Human Recombinant
IFRG28, Receptor-transporting protein 4, 3CxxC-type zinc finger protein 4, IFRG28, Z3CXXC4.
Product # :
PRO-2140Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
RTP4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 247 amino acids (1-224 a.a) and having a molecular mass of 27.8kDa.RTP4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RTP4 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Receptor Transporter Protein 4 (RTP4) is a member of the TMEM7 family.
-
Synonyms
IFRG28, Receptor-transporting protein 4, 3CxxC-type zinc finger protein 4, IFRG28, Z3CXXC4.
-
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 MGSMVVDFWT WEQTFQELIQ EAKPRATWTL KLDGNLQLDC LAQGWKQYQQ RAFGWFRCSS CQRSWASAQV QILCHTYWEH WTSQGQVRMR LFGQRCQKCS WSQYEMPEFS SDSTMRILSN LVQHILKKYY GNGTRKSPEM PVILEVSLEG SHDTANCEAC TLGICGQGLK SCMTKPSKSL LPHLKTGNSS PGIGAVYLAN QAKNQSAEAK EAKGSGYEKL GPSRDPD.
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 :
SGCB HumanDescription:
Sarcoglycan Beta Human Recombinant
Beta-sarcoglycan, Beta-SG, 43 kDa dystrophin-associated glycoprotein, 43DAG, A3b, LGMD2E, Sarcoglycan, Beta (43kDa Dystrophin-Associated Glycoprotein), Limb Girdle Muscular Dystrophy 2E (Non-Linked Families), SGC.
Product # :
PRO-2211Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SGCB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 255 amino acids (87-318 a.a) and having a molecular mass of 27.8kDa.SGCB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SGCB protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer(pH8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Sarcoglycan Beta, also known as SGCB, is a part of the sarcoglycan family. SGCB belongs to the sarcoglycan complex which is a subcomplex of the dystrophin-glycoprotein complex that connects between the F-actin cytoskeleton and the extracellular matrix.
-
Synonyms
Beta-sarcoglycan, Beta-SG, 43 kDa dystrophin-associated glycoprotein, 43DAG, A3b, LGMD2E, Sarcoglycan, Beta (43kDa Dystrophin-Associated Glycoprotein), Limb Girdle Muscular Dystrophy 2E (Non-Linked Families), SGC.
-
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 MGSWAVIRIG PNGCDSMEFH ESGLLRFKQV SDMGVIHPLY KSTVGGRRNE NLVITGNNQP IVFQQGTTKL SVENNKTSIT SDIGMQFFDP RTQNILFSTD YETHEFHLPS GVKSLNVQKA STERITSNAT SDLNIKVDGR AIVRGNEGVF IMGKTIEFHM GGNMELKAEN SIILNGSVMV STTRLPSSSS GDQLGSGDWV RYKLCMCADG TLFKVQVTSQ NMGCQISDNP CGNTH.
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 :
LDL HumanDescription:
Low-Density Lipoprotein Human
Low Density Lipoprotein, LDL.
Product # :
PRO-562Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- More Info
Description
Human Low Density Lipoprotein (LDL) produced in Human plasma.
Source
Human plasma.
More Info
-
Introduction
LDL is a low-density lipoprotein that transports cholesterol and triglycerides from the liver to peripheral tissues. LDL (like all lipoproteins) facilitates the movement of fats and cholesterol within the water based solution of the blood stream. Each natural LDL particle contains a single Apo B-100 molecule (apolipoprotein B-100 is a protein with 4536 amino acid residues) that circulates the fatty acids and keeps them soluble in the aqueous environment. Additionally, the LDL core is highly-hydrophobic, consisting of linoleate (a polyunsaturated fatty acid) and about 1500 esterified cholesterol molecules. This core is enclosed by a shell of phospholipids and unesterified cholesterol in addition to a single copy of B-100 large protein (514 kD). Even though the LDL particles are approximately 22 nm in diameter and have a mass of about 3 million Daltons, they have a mass and size distribution since the LDL particles contain a varying number of fatty acids. LDL receptors are synthesized and placed in the plasma membrane when a cell requires cholesterol. The LDL receptors scatter freely until they link to clathrin-coated pits. LDL particles in the blood stream attach to these extracellular LDL receptors. The clathrin-coated pits at that time form vesicles that are endocytosed into the cell. Once the clathrin coat is dropped, the vesicles transport the LDL and their receptors to early endosomes, onto late endosomes to lysosomes. At this point the cholesterol esters in the LDL are hydrolysed. The LDL receptors are recovered back to the plasma membrane. Since LDLs convey cholesterol to the arteries and can be retained there by arterial proteoglycans initializing the formation of plaques, increased levels are linked to atherosclerosis, and thus heart attack, stroke, and peripheral vascular disease. And so, cholesterol within LDL lipoproteins is habitually called "bad" cholesterol. This is a misconception since the cholesterol transported on LDL is the same as the one transported on other lipoprotein particles, it is in itself not "bad", rather it is how and where the cholesterol is being transported, and in what amounts ultimately, which causes adverse effects. HDL / LDL ratio can give an indication of risk for arteriosclerosis.
-
Synonyms
Low Density Lipoprotein, LDL.
-
Physical Appearance
Yellow to orange liquid.
-
Stability
Human LDL although stable at 4°C for 1 week, should be stored below -15°C (short term i.e. < 3 months) and below -70°C for long term.Human LDL can be further diluted with saline + 15% sucrose.
-
Human Virus Test
Starting material donor tested and found negative for HIV I & II antibodies, Hepatitis B surface antigen, and Hepatitis C antibodies and Syphilis, HIV1 / HCV / HBV NAT.
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 :
ACTA1 AntibodyDescription:
Actin, Mouse Anti Human
ACTA, Actin, actin, alpha 1, skeletal muscle, alpha skeletal muscle actin, alpha skeletal muscle, alpha-actin-1, ASMA, CFTD, CFTDM, MPFD, NEM1, NEM2, NEM3.
Product # :
ANT-749Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
-
Introduction
Actin is one of the most highly-conserved proteins, differing by no more than 20% in species as diverse as algae and humans .Actin or ACTA is aprotein localized in the I band of the myofibrils in the muscle, Acting together with myosin.Actin takes part in the contraction and relaxation of muscle. Actin exists as a monomer in low salt concentrations, but filaments form rapidly as salt concentration rises, with the consequent hydrolysis of ATP.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. It occurs in globular (G-actin) and fibrous (F-actin) forms. Actin is found in all eukaryotic cells (except for nematode sperm). Its other activitiessuch as cell motility, cell division and cytokinesis, vesicle and organelle movement, cell signaling, and the establishment and maintenance of cell junctions and cell shape.
-
Synonyms
ACTA, Actin, actin, alpha 1, skeletal muscle, alpha skeletal muscle actin, alpha skeletal muscle, alpha-actin-1, ASMA, CFTD, CFTDM, MPFD, NEM1, NEM2, NEM3.
-
Physical Appearance
Sterile filtered colorless solution.
-
Immunogen
Anti-human ACTA1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human ACTA1 amino acids 13-377 purified from E. coli.
-
Ig Subclass
Mouse IgG2a heavy chain and κ light chain.
-
Clone
PAT2F5AT.
-
Applications
ACTA1 antibody has been tested by ELISA, Western blot analysis and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
-
Type
Mouse Anti Human Monoclonal.
-
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
-
Purification Method
ACTA1 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL18 AntibodyDescription:
Interleukin-18, Mouse Anti Human
Interferon-gamma-inducing factor, IGIF, IL-1g, IL-18, IL1F4, MGC12320, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma, Iboctadekin.
Product # :
ANT-212Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml in PBS (after reconstitution).
More Info
-
Introduction
IL-18 is a proinflammatory cytokine. This cytokine can induce the IFN-gamma production of T cells. The combination of this cytokine and IL12 has been shown to inhibit IL4 dependent IgE and IgG1 production, and enhance IgG2a production of B cells. IL-18 binding protein (IL18BP) can specifically interact with this cytokine, and thus negatively regulate its biological activity.
-
Synonyms
Interferon-gamma-inducing factor, IGIF, IL-1g, IL-18, IL1F4, MGC12320, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma, Iboctadekin.
-
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
-
Immunogen
r.Human IL-18.
-
Ig Subclass
Mouse IgG1.
-
Clone
YNR-HIL18.
-
Applications
Direct ELISA, Western Blot, Immuneprecipitation.
-
Titer
By direct ELISA, 1:10,000 dilution will yield 0.8 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 :
NPPA HumanDescription:
Natriuretic Peptide A Human Recombinant
Natriuretic peptides A, CDD-ANF, Cardiodilatin, CDD, Cardiodilatin-related peptide, CDP, N-terminal proatrial natriuretic peptide, ANP, PND.
Product # :
CYT-1028Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
NPPA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 26-123) containing 106 amino acids including an 8 a.a N-terminal His tag. The total molecular mass is 11.7kDa (calculated).
Source
Escherichia Coli.
Formulation
NPPA filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20 mM Tris buffer, 50 mM NaCl and 5% w/v trehalosa, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Natriuretic Peptide A (NPPA) is a part of the natriuretic peptide family and is involved in cardiovascular homeostasis through regulation of natriuresis, diuresis, and vasodilation. NPPA is synthesized as a great precursor which releases a peptide from the N-terminus with similarity to vasoactive peptide, cardiodilatin, and another peptide from the C-terminus with natriuretic-diuretic activity. In female pregnancy, NPPA is promoting trophoblast invasion and spiral artery remodeling in uterus.
-
Synonyms
Natriuretic peptides A, CDD-ANF, Cardiodilatin, CDD, Cardiodilatin-related peptide, CDP, N-terminal proatrial natriuretic peptide, ANP, PND.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
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. NPPA is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
MKHHHHHHNP MYNAVSNADL MDFKNLLDHL EEKMPLEDEV VPPQVLSEPN EEAGAALSPL PEVPPWTGEV SPAQRDGGAL GRGPWDSSDR SALLKSKLRA LLTAPR.
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 :
CUTA HumanDescription:
CutA Divalent Cation Tolerance Homolog Human Recombinant
ACHAP, C6orf82, MGC111154, cutA divalent cation tolerance homolog, CUTA.
Product # :
PRO-812Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CUTA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 156 amino acids (33-179 a.a.) and having a molecular mass of 17.1 kDa. CUTA protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
CUTA Human solution containing 20mM Tris-HCl pH-8, 1mM DTT, and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
CUTA is the 179 amino acid mammalian homolog of the cutA E. coli protein and is ubiquitously expressed, particularly in brain tissue. CUTA participates in cellular tolerance to a broad range of divalent cations other than copper. The CUTA protein is a cytoplasmic protein, encoded by the single-gene operon and has been related to divalent cation tolerance.
-
Synonyms
ACHAP, C6orf82, MGC111154, cutA divalent cation tolerance homolog, CUTA.
-
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). Please prevent freeze thaw cycles.
-
Amino Acid Sequence
MRLLLLPRVL LTMASGSPPT QPSPASDSGS GYVPGSVSAA FVTCPNEKVA KEIARAVVEK RLAACVNLIP QITSIYEWKG KIEEDSEVLM MIKTQSSLVP ALTDFVRSVH PYEVAEVIAL PVEQGNFPYL QWVRQVTESV SDSITVLPLE HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TXN1 Human, HisDescription:
Thioredoxin Human Recombinant, His Tag
Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.
Product # :
PRO-804Price :
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 125 amino acids (1-105 a.a.) and having a molecular mass of 13.9 kDa (Molecular weight on SDS-PAGE will appear higher). TXN protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
TXN1 solution containing 1x PBS pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is 7-10 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
MGSSHHHHHH SSGLVPRGSH MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVIFLEVDVD DCQDVASECE VKCMPTFQFF KKGQKVGEFS 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.
- View Data Sheet
Name :
Leptin-B TilapiaDescription:
Leptin-B Tilapia Recombinant
Product # :
CYT-1110Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Leptin-B Tilapia Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids and having a molecular mass of 15,243 Dalton. The Leptin-B Tilapia is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing NaHCO3 at 1:2 salt: protein ratio.
Purity
Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Tilapia leptins were found to be biologically active in promoting proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor, but their activity was lower than that of mammalian leptin. Furthermore, the Tilapia leptins were biologically active in promoting STAT‐LUC activation in COS7 cells transfected with Tilapia leptin receptor but not in cells transfected with human leptin receptor. Tilapia Leptin A was more active than Tilapia Leptin B.
More Info
-
Introduction
Leptin is a protein hormone. It is mainly produced in adipose cells that regulate energy homeostasis by restraining hunger. Leptin ties to nuclear receptors in the hypothalamus (arcuate nucleus). Similar to insulin resistance in type II diabetes, in obesity there is a decrease in the sensitivity towards leptin, ending in a failure to identify satiety, even in high levels of energy stores or leptin itself. Full-length cDNA encoding 2 leptin sequences (tLepA and tLepB) and 1 leptin receptor sequence (tLepR) exists in tilapia (Oreochromis niloticus). The full-length cDNA of tLepR is 3423 bp, encoding a protein of 1140 amino acid which contained all functionally important domains conserved among vertebrate leptin receptors. The cDNAs of tLepA and tLepB are 486 bp and 459 bp in length, encoding proteins of 161 aa and 152 aa, respectively. The three-dimensional structures of tLepA and tLepB demonstrates strong conservation of tertiary structure with that of human leptin comprised of 4 helixes.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Leptin-B Tilapia although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin-B Tilapia 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 Leptin-B Tilapia in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The first six N-terminal amino acids of recombinant Tilapia leptin B are Ala-Leu-Leu-Thr-Lys-Gly.
-
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.19 for 1 mg/ml Leptin-B Tilapia as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.
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-12 HumanDescription:
Interleukin-12 Human Recombinant
NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.
Product # :
CYT-101Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Interleukin-12 Human Recombinant produced in HEK cells is a glycosylated heterodimer, having a total molecular weight of 57kDa.The IL12 is purified by proprietary chromatographic techniques.
Source
HEK.
Formulation
IL12 was lyophilized from a 0.2µm filtered solution containing 1xPBS.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
The specific activity was determined by the dose-dependent release of IFN-gamma from the human NK92 cell line in presence of 20ng/mL rIL-2.
The EC50 is 0.5ng/ml.More Info
-
Introduction
IL-12 is a heterodimeric cytokine that stimulates the production of IFNgamma from T-cells and natural killer cells, and also induces differentiation of Th1 helper cells. IL-12 is an initiator of cell-mediated immunity.
-
Synonyms
NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized IL-12 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL12 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 IL12 in sterile PBS containing 0.1% endotoxin-free recombinant HSA.
-
Amino Acid Sequence
IL-12 is a heterodimer of IL-12A and IL-12B linked through a disulfide-bond between cysteines in red in sequences below.
>IL-12 A
RNLPVATPDPGMFPCLHHSQNLLRAVSNMLQKARQTLEFYPCTSEEIDHEDITKDKTSTVEACLP
LELTKNESCLNSRETSFITNGSCLASRKTSFMMALCLSSIYEDLKMYQVEFKTMNAKLLMDPKRQ
IFLDQNMLAVIDELMQALNFNSETVPQKSSLEEPDFYKTKIKLCILLHAFRIRAVTIDRVMSYLNAS.
>IL-12B
IWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTLDQSSEVLGSGKTLTIQVKEFGDAG
QYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQKEPKNKTFLRCEAKNYSGRFTCWWLTTISTD
LTFSVKSSRGSSDPQGVTCGAATLSAERVRGDNKEYEYSVECQEDSACPAAEESLPIEVMVDAV
HKLKYENYTSSFFIRDIIKPDPPKNLQLKPLKNSRQVEVSWEYPDTWSTPHSYFSLTFCVQVQGK
SKREKKDRVFTDKTSATVICRKNASISVRAQDRYYSSSWSEWASVPCS.
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 :
MBL2 HumanDescription:
Mannose-Binding Lectin 2 Human Recombinant
COLEC1, HSMBPC, MBL, MBL2D, MBP, MBP-C, MBP1, Mannose-binding protein C, Collectin-1, Mannan-binding protein, Mannose-binding lectin.
Product # :
PRO-1285Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
MBL2 Human Recombinant produced in E. coli is a single polypeptide chain containing 164 amino acids (108-248) and having a molecular mass of 18 kDa. MBL2 is fused to 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The MBL2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea, 20% glycerol and 0.2M Nacl.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Mannose-binding protein C (MBL2),belongs to the collectin family of patternrecognition molecules and is an important component in the innate immune system. MBL2 is a secreted glycoprotein which recognizes mannose and N-acetylglucosamine on various microorganisms, and is capable of activating the classical complement pathway. Lacking MBL2 has been associated with susceptibility to autoimmune and infectious diseases.
-
Synonyms
COLEC1, HSMBPC, MBL, MBL2D, MBP, MBP-C, MBP1, Mannose-binding protein C, Collectin-1, Mannan-binding protein, Mannose-binding lectin.
-
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 MGSAASERKA LQTEMARIKK WLTFSLGKQV GNKFFLTNGE IMTFEKVKAL CVKFQASVAT PRNAAENGAI QNLIKEEAFL GITDEKTEGQ FVDLTGNRLT YTNWNEGEPN NAGSDEDCVL LLKNGQWNDV PCSTSHLAVC EFPI.
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 :
IL1A Human, His ActiveDescription:
Interleukin-1 alpha Human Recombinant, His Tag Active
Interleukin-1 alpha, IL-1 alpha, Hematopoietin-1, Interleukin-1 alpha: Interleukin-1a, IL-1a, Interleukin-1 alpha, IL1A, interleukin 1 alpha, IL1F1, IL-1A, preinterleukin 1 alpha, pro-interleukin-1-alpha.
Product # :
CYT-1134Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
IL1A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (113-271 a.a) and having a molecular mass of 22.4kDa. IL1A is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
IL1A protein solution (1mg/ml) contains 20mM Tris-HCl (pH 7.5) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using D10.G4.1 mouse helper T cell. The ED50 for this effect is less or equal to 0.04 ng/ml.
More Info
-
Introduction
IL-1 alpha is derived fromactivated macrophages. IL1A proteins take part in the inflammatory response, being identified as endogenous pyrogens, and stimulate the release of prostaglandin and collagenase from synovial cells.IL-1 alpha stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity.
-
Synonyms
Interleukin-1 alpha, IL-1 alpha, Hematopoietin-1, Interleukin-1 alpha: Interleukin-1a, IL-1a, Interleukin-1 alpha, IL1A, interleukin 1 alpha, IL1F1, IL-1A, preinterleukin 1 alpha, pro-interleukin-1-alpha.
-
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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMSA PFSFLSNVKY NFMRIIKYEF ILNDALNQSI IRANDQYLTA AALHNLDEAV KFDMGAYKSS KDDAKITVIL RISKTQLYVT AQDEDQPVLL KEMPEIPKTI TGSETNLLFF WETHGTKNYF TSVAHPNLFI ATKQDYWVCL AGGPPSITDF QILENQA.
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 :
DEFB116 HumanDescription:
Beta Defensin 116 Human Recombinant
Beta-Defensin 16, DEFB-16, Beta 16, defensin, Beta-Defensin 116, Defensin, Beta 16, DEFB16.
Product # :
CYT-713Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- sds-page
Description
DEFB116 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 102 amino acids (24-102 a.a) and having a molecular mass of 11.5kDa.DEFB116 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DEFB116 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
sds-page
More Info
-
Introduction
Beta Defensin 116, also known as DEFB116 is a member of the beta-defensin family.DEFB116 has antibacterial activity. The innate immune system includes antimicrobial peptides that protect multicellular organisms from a diverse spectrum of microorganisms. In addition, Beta-Defensins contain one important family of mammalian antimicrobial peptides.
-
Synonyms
Beta-Defensin 16, DEFB-16, Beta 16, defensin, Beta-Defensin 116, Defensin, Beta 16, DEFB16.
-
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 MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.
-
Background
Title: Beta Defensin 116 Human Recombinant: An Insight into its Antimicrobial Properties and Therapeutic Applications
Abstract:
Beta defensin 116 (BD116) is a key member of the beta defensin family, known for its potent antimicrobial activity against various pathogens. This research paper provides an in-depth analysis of human recombinant BD116, focusing on its production, characterization, and potential applications in antimicrobial therapy. The paper highlights the significance of BD116 in innate immunity and its role in combating microbial infections. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant BD116 in various infectious diseases. The information presented in this paper aims to enhance our understanding of human recombinant BD116 and its utility as a research tool and a potential antimicrobial agent.Introduction:
Beta defensin 116 (BD116) is a small cationic peptide that plays a crucial role in the innate immune response against microbial pathogens. Human recombinant BD116, produced through genetic engineering techniques, offers a valuable tool for studying its antimicrobial properties and exploring its therapeutic potential.Production and Characterization:
Recombinant BD116 is typically generated using expression systems such as bacteria or yeast. The protein is then purified and characterized to ensure its structural integrity and antimicrobial activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant BD116.Antimicrobial Properties:
BD116 exhibits broad-spectrum antimicrobial activity against bacteria, fungi, and viruses. It functions by disrupting the microbial cell membrane and interfering with essential cellular processes. Recombinant BD116 serves as a valuable tool for investigating the mechanisms underlying its antimicrobial action and exploring its potential as an antimicrobial agent.Therapeutic Implications:
The emergence of multidrug-resistant pathogens poses a significant challenge in the treatment of infectious diseases. Recombinant BD116 holds promise as an alternative therapeutic option due to its potent antimicrobial properties. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant BD116 in various infectious diseases, including bacterial skin infections and respiratory tract infections.Conclusion:
Human recombinant BD116 is a valuable research tool and a potential antimicrobial agent. Its production, characterization, and applications in antimicrobial therapy contribute to our understanding of innate immunity and the development of novel therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant BD116 offer promising prospects for combating multidrug-resistant pathogens and improving outcomes in infectious diseases.What is the molecular weight/Mw of DEFB116 Protein?
DEFB116 Protein has a total Mw of 11.5kDa.
What is the source or expression system of DEFB116 Protein?
Escherichia Coli.
What is the Purity of DEFB116 Protein?
DEFB116 Protein is >80% pure as determined by SDS-PAGE.
What is the Biological Activity of DEFB116 Protein?
The biological functionality of DEFB116 Protein will be determined in the future.
What is the amino acid sequence of DEFB116 Protein?
MGSSHHHHHH SSGLVPRGSH MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.
What applications can DEFB116 Protein be used in?
DEFB116 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for DEFB116 Protein?
The endotoxin level is minimal, DEFB116 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 :
DLL4 HumanDescription:
Delta-Like 4 Human Recombinant
Delta-like protein 4, Drosophila Delta homolog 4, Delta4, delta like canonical Notch ligand 4, AOS6, hdelta2.
Product # :
PRO-2660Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
DLL4 Human Recombinant produced in HEK293 is a single glycosylated polypeptide chain containing 504 amino acids (27-529 a.a) and having a molecular mass of 55.1kDa. DLL4 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293.
Formulation
DLL4 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Delta-Like4 or DLL4 is implicated in the Notch signaling transduction as Notch ligand. DLL4 down regulates endothelial cell proliferation, migration and angiogenic sprouting. DLL4 is crucial for retinal progenitor proliferation &furthermore required for suppressing rod fates in late retinal progenitors & for proper generation of other retinal cell types. Also, at some stages in the spinal cord neurogenesis, DLL4 inhibits V2a interneuron fate.
-
Synonyms
Delta-like protein 4, Drosophila Delta homolog 4, Delta4, delta like canonical Notch ligand 4, AOS6, hdelta2.
-
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
SGVFQLQLQE FINERGVLAS GRPCEPGCRT FFRVCLKHFQ AVVSPGPCTF GTVSTPVLGT NSFAVRDDSS GGGRNPLQLP FNFTWPGTFS LIIEAWHAPG DDLRPEALPP DALISKIAIQ GSLAVGQNWL LDEQTSTLTR LRYSYRVICS DNYYGDNCSR LCKKRNDHFG HYVCQPDGNL SCLPGWTGEY CQQPICLSGC HEQNGYCSKP AECLCRPGWQ GRLCNECIPH NGCRHGTCST PWQCTCDEGW GGLFCDQDLN YCTHHSPCKN GATCSNSGQR SYTCTCRPGY TGVDCELELS ECDSNPCRNG GSCKDQEDGY HCLCPPGYYG LHCEHSTLSC ADSPCFNGGS CRERNQGANY ACECPPNFTG SNCEKKVDRC TSNPCANGGQ CLNRGPSRMC RCRPGFTGTY CELHVSDCAR NPCAHGGTCH DLENGLMCTC PAGFSGRRCE VRTSIDACAS SPCFNRATCY TDLSTDTFVC NCPYGFVGSR CEFPVGLPHH 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 alpha MouseDescription:
Interleukin-1 alpha Mouse Recombinant
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.
Product # :
CYT-523Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Interleukin-1A Mouse Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 156 amino acids and having a molecular mass of 17.9 kDa. The IL-1A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS, pH=7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of murine D10S cells is < 0.002 ng/ml.More Info
-
Introduction
Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.
-
Synonyms
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Interleukin-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1A 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 Interleukin 1a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
SAPYTYQSDL RYKLMKLVRQ KFVMNDSLNQ TIYQDVDKHY LSTTWLNDLQ QEVKFDMYAY SSGGDDSKYP VTLKISDSQL FVSAQGEDQP VLLKELPETP KLITGSETDL IFFWKSINSK NYFTSAAYPE LFIATKEQSR VHLARGLPSM TDFQIS.
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 alpha Rat, HisDescription:
Interleukin-1 alpha Rat Recombinant, His Tag
Interleukin-1 alpha, IL-1 alpha.
Product # :
CYT-913Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
IL 1 alpha Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids (115-270 a.a) and having a molecular mass of 20.2kDa. IL 1 alpha is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL 1 alpha protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The biological activity was Rat IL1 alpha was measured in a cell proliferation assay using D10.G4.1 mouse helper T cell. The ED50 for this effect is less or equal to 20 pg/ml.
More Info
-
Introduction
IL-1 alpha is produced by activated macrophages, stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1A 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
Interleukin-1 alpha, IL-1 alpha.
-
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 MGSSAPHSFQ NNLRYKLIRI VKQEFIMNDS LNQNIYVDMD RIHLKAASLN DLQLEVKFDM YAYSSGGDDS KYPVTLKVSN TQLFVSAQGE DKPVLLKEIP ETPKLITGSE TDLIFFWEKI NSKNYFTSAA FPELLIATKE QSQVHLARGL PSMIDFQIS.
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 12 p40 HumanDescription:
Interleukin-12 p40 Human Recombinant
NKSF2, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 40 kDa subunit (CLMF p40), TSF, Edodekin-alpha, IL-12 p40, IL-12B, IL-12 subunit p40, NK cell stimulatory factor chain 2.
Product # :
CYT-488Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Interleukin-12 p40 His Human Recombinant produced in E.Coli is single, a non-glycosylated, polypeptide chain containing 306 amino acids fragment (23-328) with an amino-terminal hexahistidine tag. The IL-12 p40 His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Interleukin-12 p40 His is supplied in 1xPBS and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Active IL-12 is a p70 disulphide-linked dimer composed of p35 and p40 subunits. The protein is a pleiotropic cytokine produced primarily by antigen presenting cells and has multiple effects on T lymphocytes and natural killer cells in terms of stimulating cytotoxicity, proliferation, production of other cytokines and Th1 subset differentiation.
-
Synonyms
NKSF2, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 40 kDa subunit (CLMF p40), TSF, Edodekin-alpha, IL-12 p40, IL-12B, IL-12 subunit p40, NK cell stimulatory factor chain 2.
-
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. Please avoid 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 :
Omentin HumanDescription:
Omentin Human Recombinant
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
Product # :
CYT-301Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Omentin Human Recombinant is produced in E.Coli by recombinant DNA technology is a single, polypeptide chain containing 313 amino acids and having a molecular mass of 35 kDa. Intelectin is purified by proprietary chromatographic techniques.
Source
E.Coli.
Formulation
Each mg of lyophilized powder contains 10mM NaP, pH-7.5 and 5:1 mannitol to protein.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Omentin is a recently recognized gene highly localized to the mental tissue (visceral adipose tissue). Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase INSstimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of INS presence. Its role in glucose metabolism and obesity remains to be described; an INS-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.
-
Synonyms
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Intelectin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Intelectin 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 Omentin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MNQLSFLLFL IATTRGWSTD EANTYFKEWTCSSSPSLPRS CKEIKDECPS AFDGLYFLRT ENGVIYQTFC DMTSGGGGWT LVASVHENDM RGKCTVGDRW SSQQGSKADY PEGDGNWANY NTFGSAEAAT SDDYKNPGYY DIQAKDLGIW HVPNKSPMQH WRNSSLLRYR TDTGFLQTLG HNLFGIYQKY PVKYGEGKCW TDNGPVIPVV YDFGDAQKTA SYYSPYGQRE FNNERAANAL CAGMRVTGCN TEHHCIGGGG YFPEASPQQC GDFSGFDWSG YGTHVGYSSS REITEAAVLLFYR.
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 22 HumanDescription:
Interleukin-22 Human Recombinant
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
Product # :
CYT-328Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Interleukin-22 Human Recombinant produced in E.Coli is a single, non-glycosylated homodimeric polypeptide chain containing 2 x 146 amino acids and having a total molecular mass of 33,607 Dalton. The IL-22 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Each mg contains 50mM Phosphate buffer pH=7.1.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Biological Activity was determined by the ability to activiate STAT following receptor ligand interaction.More Info
-
Introduction
IL-22 is a member of the IL-10 family of regulatory cytokines.Members of this family share partial homology in their amino acid sequences, but they are dissimilar in their biological functions. Produced by T lymphocytes, IL-22 inhibits IL-4 production by Th2 cells, and induces acute phase reactants in the liver and pancreas. IL-22 signals through a receptor system consisting of IL-10R-beta/CRF2-4 and IL-22R, both of which are members of the class II cytokine-receptor family.
-
Synonyms
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Interleukin-22 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL22 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 Interleukin -22 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Pro-Ile-Ser.
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 28A Human, HisDescription:
Interleukin-28A Human Recombinant, His Tag
Interleukin-28A, IL-28A, IFN-Lambda 2, Interferon-Lambda 2, Cytokine ZCYTO20, IL28A, IFNL2, ZCYTO20.
Product # :
CYT-813Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
IL 28A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids (26-200 a.a.) and having a molecular mass of 22.1kDa. IL 28A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL 28A protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
IL-28A is distantly related to type I interferons and the IL-10 family. Expression of IL-28A is induced by viral infection which interacts with a heterodimeric class II cytokine receptor that consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha. IL-28A exhibits common features with type I IFNs such as antiviral activity, antiproliferative activity and in vivo antitumour activity.
IL-28A acts similarly to IFNs, but is less effective generally and has activity in a more limited range of cell lines. IFN-ambda 1, IFN-lambda 2 and IFN-lambda 3 are closely positioned genes on human chromosome 19.
IL-28A induces ELR(-) CXC chemokine mRNA in human peripheral blood mononuclear cells, in an IFN-gamma-independent manner.
IL-28A is able to generate tolerogenic DCs, an activity that could thwart IFN-beta functions. IL-28A produced in response to viral infection, activates both monocytes and macrophages producing a restricted panel of cytokines and therefore is an important factor in activating innate immune responses at the site of viral infection. -
Synonyms
Interleukin-28A, IL-28A, IFN-Lambda 2, Interferon-Lambda 2, Cytokine ZCYTO20, IL28A, IFNL2, ZCYTO20.
-
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 MGSVPVARLH GALPDARGCH IAQFKSLSPQ ELQAFKRAKD ALEESLLLKD CRCHSRLFPR TWDLRQLQVR ERPMALEAEL ALTLKVLEAT ADTDPALVDV LDQPLHTLHH ILSQFRACIQ PQPTAGPRTR GRLHHWLYRL QEAPKKESPG CLEASVTFNL FRLLTRDLNC VASGDLCV .
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 29 HumanDescription:
Interleukin-29 Human Recombinant
Interleukin-29, IL-29, IFN-Lambda 1, IFN-Lambda 1, Cytokine ZCYTO21, IL29, IFNL1, ZCYTO21.
Product # :
CYT-603Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
IL-29 human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 181 amino acids and having a molecular mass of 20 kDa.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2 μm filtered solution containing no additives.
Purity
Greater than 90% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
IL-29 is distantly related to type I IFNs and the IL-10 family. Expression of IL-29 is induced by viral infection which interacts with a heterodimeric class II cytokine receptor that consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha. IL-29 exhibits common features with type I IFNs such as antiviral activity, antiproliferative activity and in vivo antitumour activity.
IL-29 acts similarly to IFNs, but is less effective generally and has activity in a more limited range of cell lines. IFN-ambda 1, IFN-lambda 2 and IFN-lambda3 are closely positioned genes on human chromosome 19.
IL-29 induces ELR(-) CXC chemokine mRNA in human peripheral blood mononuclear cells, in an IFN-gamma-independent manner.
IL-29 is able to generate tolerogenic DCs, an activity that could thwart IFN-beta functions. IL-29 produced in response to viral infection, activates both monocytes and macrophages producing a restricted panel of cytokines and therefore is an important factor in activating innate immune responses at the site of viral infection.
IFN-Lambda 1 antiviral and antiproliferative activity requires IFN-Lambda 2 receptor tyrosine residues. -
Synonyms
Interleukin-29, IL-29, IFN-Lambda 1, IFN-Lambda 1, Cytokine ZCYTO21, IL29, IFNL1, ZCYTO21.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized IFN-Lambda 1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-Lambda 1 Recombinant should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized IL-29 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
GPVPTSKPTTT GKGCHIGRFK SLSPQELASF KKARDALEES LKLKNWSCSS PVFPGNWDLR LLQVRERPVA LEAELALTLK VLEAAAGPAL EDVLDQPLHTLHHILSQLQA CIQPQPTAGP RPRGRLHHWL HRLQEAPKKE SAGCLEASVT FNLFRLLTRD LKYVADGNLC LRTSTHPEST.
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.