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Name :
IDS AntibodyDescription:
Iduronate 2-Sulfatase, Mouse Anti Human
Iduronate 2-Sulfatase, Alpha-L-Iduronate Sulfate Sulfatase, Idursulfase, SIDS, Iduronate 2-Sulfatase 14 KDa Chain, Iduronate 2-Sulfatase 42 KDa Chain, Hunter Syndrome, EC 3.1.6.13, MPS2, Iduronate 2-sulfatase, Alpha-L-iduronate sulfate sulfatase, Idursulfase.
Product # :
ANT-745Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
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Introduction
Iduronate 2-Sulfatase also known as IDS, belongs to the highly-conserved sulfatase family of enzymes which catalyze the hydrolysis of O-sulfate and N-salfate esters from a variety of substrates. IDS is essential for the lysosomal degradation of the glycosaminoglycans (GAG) heparan sulfate as well as dermatan sulfate. Furthermore, IDS hydrolyzes the 2-sulfate group of the IDS units of the GAG.
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Synonyms
Iduronate 2-Sulfatase, Alpha-L-Iduronate Sulfate Sulfatase, Idursulfase, SIDS, Iduronate 2-Sulfatase 14 KDa Chain, Iduronate 2-Sulfatase 42 KDa Chain, Hunter Syndrome, EC 3.1.6.13, MPS2, Iduronate 2-sulfatase, Alpha-L-iduronate sulfate sulfatase, Idursulfase.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human IDS mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human IDS protein 26-550 amino acids purified from insect cell.
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Ig Subclass
Mouse IgG2b heavy chain and k light chain.
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Clone
PAT6H4AT.
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Applications
The antibody has been tested by ELISA, Western blot analysis and FACS analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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Type
Mouse Anti Human Monoclonal.
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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.
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Purification Method
IDS 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.
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Name :
ING2 AntibodyDescription:
Inhibitor of Growth Family Member 2, Mouse Anti Human
Inhibitor Of Growth Family Member 2, ING1L, Inhibitor Of Growth 1-Like Protein, P33ING2, ING1Lp, P32, Inhibitor Of Growth Family Member 1-Like, Inhibitor Of Growth Protein 2, ING2.
Product # :
ANT-513Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
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Introduction
Inhibitor of Growth Family, Member 2 (ING2) belongs to the inhibitor of growth (ING) family. ING family members associate with and modulate the activity of histone acetyltransferase (HAT) and histone deacetylase (HDAC) complexes and serve in DNA repair and apoptosis. ING2 appears to be involved in p53/TP53 activation and p53/TP53-dependent apoptotic pathways, most likely by enhancing acetylation of p53/TP53. ING2 is a component of an mSin3A-like corepressor complex, which is probably involved in deacetylation of nucleosomal histones. ING2 activity is modulated by binding to phosphoinositides (PtdInsPs).
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Synonyms
Inhibitor Of Growth Family Member 2, ING1L, Inhibitor Of Growth 1-Like Protein, P33ING2, ING1Lp, P32, Inhibitor Of Growth Family Member 1-Like, Inhibitor Of Growth Protein 2, ING2.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human ING2 mAb, clone PAT39E5AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human ING2 protein 1-280 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and k light chain.
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Clone
PAT39E5AT.
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Applications
The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.
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Type
Mouse Anti Human Monoclonal.
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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.
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Purification Method
ING2 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.
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Name :
ITAC (63-87) HumanDescription:
ITAC (63-87 a.a.) Human Recombinant
ITAC, I-TAC, CXCL-11, CXCL11.
Product # :
CHM-049Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The I-TAC Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The I-TAC His-Tagged Fusion Protein, produced in E. coli, is a 9kDa protein containing 25 amino acid residues of the I-TACHuman, 63-87 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
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Synonyms
ITAC, I-TAC, CXCL-11, CXCL11.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized I-TAC at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Background
I-TAC is a small cytokine belongs to the CXC chemokinen family which also called inducible T-cell alpha chemoattractant and IP-9. I-TAC is expressed mainly in peripheral blood leukocytes, liver and pancreas with moderate levels in spleen, thymus and lung and low levels in small intestine, placenta and prostate. IFN-g and IFN-b induces strongly gene expression of I-TAC. The I-TAC 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.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL 1 beta HumanDescription:
Interleukin-1 beta Human Recombinant
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
Product # :
CYT-208Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-1 beta Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 153 amino acids and having a molecular mass of 17000 Dalton.The IL-1 Beta is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL-1 Beta was lyophilized from a concentrated (1mg/ml) sterile solution containing 50mM Phosphate buffer pH=7.1 and 150mM NaCl.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined in the test of augmentation of lymphocyte proliferation assay using mouse thymus was found to be 200,000,000 IU/mg.More Info
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Introduction
Interleukin-1b is produced by activated macrophages, IL-1 Beta 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 from synovial cells.
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Synonyms
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-1b 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.
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Solubility
It is recommended to reconstitute the lyophilized Interleukin-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Val-Arg-Ser.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.631 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IL-1 beta Recombinant as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IFN a 2b Human, 20 kd PEGDescription:
Interferon-alpha 2b 20kd-Pegylated Human Recombinant
Interferon alpha 2b, IFNA, INFA2, MGC125764, MGC125765.
Product # :
CYT-034Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Interferon-a 2b Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 19269 Dalton. The Pegylated IFN-a 2b is produced by attaching a 20kDa mPEG-aldehyde to the N-terminal IFN alpha-2b. Interferon-a 2b is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IFN-a 2b is supplied in solution (1.48mg/ml) containing 20mM Acetate Buffer (pH 6.0), 0.8%NaCl and 0.005% Polysorbate 80.
Purity
Greater than 97.0% as determined by SEC-HPLC.
Biological Activity
The specific activity as determined in a viral resistance assay using VSV-WISH cells was found to be 3,000,000 IU/mg.
More Info
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Introduction
IFN-alpha is produced by macrophages and has antiviral activities. Interferon stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.
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Synonyms
Interferon alpha 2b, IFNA, INFA2, MGC125764, MGC125765.
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Physical Appearance
Colorless, clear and transparent solution.
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Stability
IFN alpha-2b PEG should be stored refrigerated at 2° to 8°C. Vials should be kept in their packaging to protect from light until the time of use. Shaking and freezing should be avoided.
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Background
What is the molecular weight/Mw of IFN A 2B HUMAN, 20 KD PEG Protein?
IFN A 2B HUMAN, 20 KD PEG Protein has a total Mw of 19.2kDa.
What is the source or expression system of IFN A 2B HUMAN, 20 KD PEG Protein?
Escherichia Coli.
What is the Purity of IFN A 2B HUMAN, 20 KD PEG Protein?
IFN A 2B HUMAN, 20 KD PEG Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of IFN A 2B HUMAN, 20 KD PEG Protein?
The specific activity as determined in a viral resistance assay using VSV-WISH cells was found to be 3,000,000 IU/mg.
What is the amino acid sequence of IFN A 2B HUMAN, 20 KD PEG Protein?
IFN A 2B HUMAN, 20 KD PEG Protein is composed from 165 amino acids.
What applications can IFN A 2B HUMAN, 20 KD PEG Protein be used in?
IFN A 2B HUMAN, 20 KD PEG Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFN A 2B HUMAN, 20 KD PEG Protein?
The endotoxin level is minimal, IFN A 2B HUMAN, 20 KD PEG Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
WIF1 HumanDescription:
WNT Inhibitory Factor 1 Human Recombinant
WIF1, WIF-1, Wnt inhibitory factor 1.
Product # :
PRO-684Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
WIF1 Human is a single, glycosylated polypeptide chain containing 360 amino acids (29-379 a.a.) and having a molecular mass of 39.5 kDaWIF1 is fused to 6 amino acid His Tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The WIF1 protein solution contains 1X PBS pH 7.4, 20% glycerol, 1mM DTT and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
WIF1 binds to wnt proteins and inhibits their activities. WIF1 plays a role in mesoderm segmentation. WNT proteins are extracellular signaling molecules that take part in the control of embryonic development & cancer. WIF1 protein contains a WNT inhibitory factor (WIF) domain and 5 epidermal growth factor (EGF)-like domains. WIF1 takes part in mesoderm segmentation. WIF1 protein is found to be present in fish, amphibia and mammals. WIF1 is a recurrent target in human salivary gland oncogenesis. Downregulation of WIF1 takes part in the development and progression of pleomorphic adenomas. WIF1 is a tumor suppressor, specifically in nonfunctioning pituitary tumors.
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Synonyms
WIF1, WIF-1, Wnt inhibitory factor 1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADLGPPQEES LYLWIDAHQA RVLIGFEEDI LIVSEGKMAP FTHDFRKAQQ RMPAIPVNIH SMNFTWQAAG QAEYFYEFLS LRSLDKGIMA DPTVNVPLLG TVPHKASVVQ VGFPCLGKQD GVAAFEVDVI VMNSEGNTIL QTPQNAIFFK TCQQAECPGG CRNGGFCNER RICECPDGFH GPHCEKALCT PRCMNGGLCV TPGFCICPPG FYGVNCDKAN CSTTCFNGGT CFYPGKCICP PGLEGEQCEI SKCPQPCRNG GKCIGKSKCK CSKGYQGDLC SKPVCEPGCG AHGTCHEPNK CQCQEGWHGR HCNKRYEASL IHALRPAGAQ LRQHTPSLKK AEERRDPPES NYIWHHHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
AOD-9604Description:
AOD-9604
Product # :
HOR-064Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
AOD-9604 is a synthetic single, non-glycosylated polypeptide chain containing 16 amino acids, having a molecular mass of 1815 Dalton and a Molecular formula of C78H123N23O23 S2.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized AOD-9604 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution AOD-9604 should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized AOD-9604 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
H-Tyr-Leu-Arg-Ile-Val-Gln-Cys-Arg-SerVal-Glu-Gly-Ser-Cys-Gly-Phe-OH (Disulfide bond).
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Background
AOD-9604 is a synthetic analog of the C-terminal fragment (177–191) AOD-9604 stimulates lipolysis (fat breakdown) without the unwanted growth-promoting or insulin-antagonizing effects of full-length hGH. AOD-9604 is a potent lipolytic tool in animal models and researchers focus on its regenerative properties in joint health and its ability to modulate beta3 adrenergic receptors without the systemic risks of growth hormone.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
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
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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
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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.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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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.
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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.
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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.
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Name :
Adiponectin Human, TrimericDescription:
Adiponectin Human Recombinant, Trimeric form
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-233Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Trimeric form of Adiponectin Human trimeric form was expressed in HEK293 cells. The cysteine 39 was replaced with Alanine (C39A) 9. hAd-C39A can only form a trimer, but not a hexamer or an HMW form.
Source
HEK293 (Human embryonic kidney cell line).
Formulation
Filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer, 0.075M NaCl, pH 7.4.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
ED50= 3-8.5 μg/ml, as determined by its ability to inhibit proliferation of HASMCs induced by HB EGF.
More Info
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Introduction
Adiponectin is a hormone exclusively expressed from adipose tissue.
Many studies demonstrate that Adiponectin has direct anti-diabetic, anti-atherogenic and anti-inflammatory functions. APM-1 can increase insulin sensitivity of skeletal muscle. Attenuate hepatic lipogenesis and gluconeogenesis, regulate NO production in endothelial cells, inhibit proliferation of smooth muscle cells and prevent lipid accumulation of macrophage cells.
In the circulation, Adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (MMW, also called trimer) forms 8. Different oligomeric complex of Adiponectin activates different signaling pathways and exerts distinct functions. -
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized Adiponectin at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
Add deionized water to a working volume of 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 in the cell culture.
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Amino Acid Sequence
ETTTQGPGVL LPLPKGAATG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDD DDK.
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Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 25 kDa.
What is the source or expression system of ADIPONECTIN Protein?
HEK293.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
ED50= 3-8.5 μg/ml, as determined by its ability to inhibit proliferation of HASMCs induced by HB EGF.What is the amino acid sequence of ADIPONECTIN Protein?
ETTTQGPGVL LPLPKGAATG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDD DDK.
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.
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Name :
CEA Human, HisDescription:
Carcinoembryonic Antigen Human Recombinant, His Tag
Carcinoembryonic Antigen Related Cell Adhesion Molecule 5, Carcinoembryonic Antigen-Related Cell Adhesion Molecule 5, Meconium Antigen 100, CEA, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic antigen-related cell adhesion molecule 5, Carcinoembryonic antigen, CEA.
Product # :
PRO-2407Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CEA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 659 amino acids (35-685a.a.) and having a molecular mass of 72.3kDa (Molecular size on SDS-PAGE will appear at approximately 70-150kDa). CEA is expressed with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CEA protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Carcinoembryonic antigen (CEA) is a glycoprotein present in fetal digestive-tract tissues; it’s involved in cell adhesion. The production of CEA stops before birth. CEA is called tumor marker since its elevated levels are found in the serum from individuals with colorectal, gastric, pancreatic, lung and breast carcinomas and in heavy smokers.
There are also benign conditions that elevate CEA levels such as smoking, infection, inflammatory bowel disease, pancreatitis, cirrhosis of the liver, and some benign tumors (in the equivalent organs which have cancers with elevated CEA). Typically, higher levels of CEA are found in men, smokers, and older individuals.
The presence of CEA assists in screening, in evaluating recurrent or disseminated disease, and in determining the success of surgical removal of malignant tumors.
CEA levels can be used as indicators of treatment success. The normal values range from 0.0 to 2.5 ng/ml of serum (from blood), in non-smokers, a greater amount than that may be suggestive of cancer. Levels above 20 ng/ml before treatment are associated with cancer which has already metastasized. Benign conditions do not usually cause a CEA increase over 10 ng/ml.
The high levels of CEA should return to normal after successful therapy, however if during follow up there’s an elevation in CEA levels it indicates a recurrence of tumor.
Carcinoembryonic antigen family belongs to the immunoglobulin superfamily; it consists of 29 genes, 18 of which are normally expressed. -
Synonyms
Carcinoembryonic Antigen Related Cell Adhesion Molecule 5, Carcinoembryonic Antigen-Related Cell Adhesion Molecule 5, Meconium Antigen 100, CEA, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic antigen-related cell adhesion molecule 5, Carcinoembryonic antigen, CEA.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
KLTIESTPFN VAEGKEVLLL VHNLPQHLFG YSWYKGERVD GNRQIIGYVI GTQQATPGPA YSGREIIYPN ASLLIQNIIQ NDTGFYTLHV IKSDLVNEEA TGQFRVYPEL PKPSISSNNS KPVEDKDAVA FTCEPETQDA TYLWWVNNQS LPVSPRLQLS NGNRTLTLFN VTRNDTASYK CETQNPVSAR RSDSVILNVL YGPDAPTISP LNTSYRSGEN LNLSCHAASN PPAQYSWFVN GTFQQSTQEL FIPNITVNNS GSYTCQAHNS DTGLNRTTVT TITVYAEPPK PFITSNNSNP VEDEDAVALT CEPEIQNTTY LWWVNNQSLP VSPRLQLSND NRTLTLLSVT RNDVGPYECG IQNKLSVDHS DPVILNVLYG PDDPTISPSY TYYRPGVNLS LSCHAASNPP AQYSWLIDGN IQQHTQELFI SNITEKNSGL YTCQANNSAS GHSRTTVKTI TVSAELPKPS ISSNNSKPVE DKDAVAFTCE PEAQNTTYLW WVNGQSLPVS PRLQLSNGNR TLTLFNVTRN DARAYVCGIQ NSVSANRSDP VTLDVLYGPD TPIISPPDSS YLSGANLNLS CHSASNPSPQ YSWRINGIPQ QHTQVLFIAK ITPNNNGTYA CFVSNLATGR NNSIVKSITV SASGTSPGLS ALEHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CXCL14 Human, HisDescription:
BRAK Human Recombinant (CXCL14), His-Tag
C-X-C motif chemokine 14, Small-inducible cytokine B14, Chemokine BRAK, Bolekine, NJAC, KS1, Kec, BMAC, MIP-2g, SCYB14, CXCL14, BRAK, MGC10687.
Product # :
CHM-239Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CXCL14 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 88 amino acids and having a molecular mass of 10.66 kDa. The Human BRAK contains a 10 a.a. fusion His tag at N-Terminus. The BRAK is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CXCL14 filtered (0.4µm) and lyophilized from a concentrated (0.5mg/ml) solution containing 20mM Tris buffer & 20mM NaCl pH-7.5.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
CXCL14 is involved in immunoregulatory and inflammatory processes. BRAK protein is structurally related to the CXC (Cys-X-Cys) subfamily of cytokines. CXCL14 displays chemotactic activity for monocytes but not for lymphocytes, dendritic cells, neutrophils or macrophages. CXCL14 is involved in the homeostasis of monocyte-derived macrophages.
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Synonyms
C-X-C motif chemokine 14, Small-inducible cytokine B14, Chemokine BRAK, Bolekine, NJAC, KS1, Kec, BMAC, MIP-2g, SCYB14, CXCL14, BRAK, MGC10687.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BRAK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BRAK should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CXCL14 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIITTKS VSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.
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Background
What is the molecular weight/Mw of CXCL14 HUMAN, HIS Protein?
CXCL14 HUMAN, HIS Protein has a total Mw of 10.66kDa.
What is the source or expression system of CXCL14 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CXCL14 HUMAN, HIS Protein?
CXCL14 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL14 HUMAN, HIS Protein?
The biological functionality of CXCL14 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CXCL14 HUMAN, HIS Protein?
MKHHHHHHAS SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIITTKS VSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.
What applications can CXCL14 HUMAN, HIS Protein be used in?
CXCL14 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL14 HUMAN, HIS Protein?
The endotoxin level is minimal, CXCL14 HUMAN, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
StreptavidinDescription:
Streptavidin Recombinant
Product # :
PRO-791Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Streptavidin Streptomyces Avidinii Recombinant produced in E.Coli. The molecular weight per tetramer is approximately 52kDa.
Source
Escherichia Coli.
Formulation
Lyophilized in 10mM potassium phosphate buffer pH 6.5.
Purity
Greater than 98.0% as determined by SDS-PAGE and HPLC.
More Info
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Introduction
Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is widely used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Streptavidin is shipped at ambient temperature, upon arrival store at -20°C.
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Solubility
It is recommended to reconstitute the lyophilized Streptavidin in sterile 18MΩ-cm H2O not less than 0.5mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MAEAGITGTWYNQLGSTFIVTAGADGALTGTYESAVGNAESRYVLT
GRYDSAPATDGSGTALGWTVAWKNNYRNAHSATTWSGQYVGGA
EARINTQWLLTSGTTEANAWKSTLVGHDTFTKVKPSAAS. -
Proteolytic Activity
< 10-3 U/mg protein (Azocoll, 25 °C, 24 h, pH 8.0).
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Specific Activity
> 17U/mg (one unit binds 1 μg D-biotin).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL 11 Human, PichiaDescription:
Interleukin-11 Human Recombinant, Pichia
Interleukin-11, IL-11, Adipogenesis inhibitory factor, AGIF, Oprelvekin, IL11.
Product # :
CYT-013Price :
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Shipped at Room temp
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Description
IL11 Human Recombinant produced in Pichia Pastoris is a single, non-glycosylated, Polypeptide chain containing 177 amino acids (it differs from the 178 amino acid length of the native IL11 only in lack of the N-terminal praline residue) and having a molecular mass of 19kDa.The IL11 is purified by proprietary chromatographic techniques.
Source
Pichia Pastoris.
Formulation
IL11 was Lyophilized from a 0.2 µm filtered concentrated solution of 20mM PB, pH7.2 and 2% Glycine buffer.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by the dose-dependent stimulation of the proliferation of murine 7TD1 was found to be less then 0.2ng-0.8ng/ml, corresponding to a Specific Activity of greater than 1,000,000 IU/ mg.
More Info
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Introduction
IL11 is a member of the gp130 family of cytokines. These cytokines drive the assembly of multisubunit receptor complexes, all of which contain at least one molecule of the transmembrane signaling receptor IL6ST (gp130). IL-11 is shown to stimulate the T-cell-dependent development of immunoglobulin-producing B cells. It is also found to support the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells.
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Synonyms
Interleukin-11, IL-11, Adipogenesis inhibitory factor, AGIF, Oprelvekin, IL11.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IL11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL11 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interleukin -11 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Pro-Pro-Pro-Gly.
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 :
SNCA A30P HumanDescription:
Alpha Synuclein A30P Human Recombinant
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
Product # :
PRO-158Price :
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Shipping Method :
Shipped with Ice Packs
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Description
A-Synuclein A30P Human Recombinant which is a Parkinson’s disease-related point mutant, produced in E.Coli is a single, non-glycosylated polypeptide chain of 140 amino acids having a molecular mass of 14.4kDa (molecular size on SDS-PAGE will appear higher). The Recombinant Human a-Synuclein A30P is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SNCA A30P protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).
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Synonyms
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAP GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CAMP HumanDescription:
Cathelicidin Antimicrobial Peptide Human Recombinant
CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.
Product # :
PRO-1405Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CAMP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (34-173 a.a.) and having a molecular mass of 18.4kDa.CAMP is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
CAMP protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
CAMP belongs to the antimicrobial peptide family, contains highly conserved N-terminal signal peptide, a cathelin domain and a structurally variable cationic antimicrobial peptide that produced by extracellular proteolysis from the C-terminus. CAMP has numerous functions besides the antimicrobial activity such as: cell chemotaxis, immune mediator induction and inflammatory response regulation.
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Synonyms
CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQVLSYKE AVLRAIDGIN QRSSDANLYR LLDLDPRPTM DGDPDTPKPV SFTVKETVCP RTTQQSPEDC DFKKDGLVKR CMGTVTLNQA RGSFDISCDK DNKRFALLGD FFRKSKEKIG KEFKRIVQRI KDFLRNLVPR TES.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
OCT HumanDescription:
Octreotide Human
Product # :
HOR-265Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Octreotide Human Synthetic is a single, non-glycosylated, polypeptide chain containing 8 amino acids, having a molecular mass of 1019.26 Dalton and a molecular formula of C49H66N10O10S2.Octreotide is purified by proprietary chromatographic techniques.
Formulation
The Octreotide was lyophilized from a concentrated (1mg/ml) solution with no additives.
Purity
Greater than 98.0% as determined by RP-HPLC.
More Info
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Introduction
Octreotide acetate is a longer acting synthetic octapeptide analog of naturally occurring somatostatin. It inhibits the secretion of gastro-entero-pancreatic peptide hormones and the release of growth hormone.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Octreotide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Octreotide should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Octreotide in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
H-D-Phe-Cys-Phe-D-Trp-Lys-Thr-Cys-L-threoninol.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GID8 HumanDescription:
GID Complex Subunit 8 Human Recombinant
GID Complex Subunit 8, C20orf11, TWA1, Two Hybrid-Associated Protein 1 With RanBPM,GID Complex Subunit 8 Homolog (S. Cerevisiae), Glucose-Induced Degradation Protein 8 Homolog, Chromosome 20 Open Reading Frame 11, GID Complex Subunit 8 Homolog, Protein C20orf11, GID8.
Product # :
PRO-2191Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GID8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 251 amino acids (1-228 a.a) and having a molecular mass of 29.1kDa.GID8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GID8 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
GID Complex Subunit 8, also known as GID8 is a member of the GID8 family. GID8 was recognized through a two hybrid-associated protein screen with RanBPM. GID8 acts together with RanBP9 and includes a protein complex with RanBPM and Muskelin.
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Synonyms
GID Complex Subunit 8, C20orf11, TWA1, Two Hybrid-Associated Protein 1 With RanBPM,GID Complex Subunit 8 Homolog (S. Cerevisiae), Glucose-Induced Degradation Protein 8 Homolog, Chromosome 20 Open Reading Frame 11, GID Complex Subunit 8 Homolog, Protein C20orf11, GID8.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSYAEKP DEITKDEWME KLNNLHVQRA DMNRLIMNYL VTEGFKEAAE KFRMESGIEP SVDLETLDER IKIREMILKG QIQEAIALIN SLHPELLDTN RYLYFHLQQQ HLIELIRQRE TEAALEFAQT QLAEQGEESR ECLTEMERTL ALLAFDSPEE SPFGDLLHTM QRQKVWSEVN QAVLDYENRE STPKLAKLLK LLLWAQNELD QKKVKYPKMT DLSKGVIEEP K
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
H3N2 Switzerland RecombinantDescription:
H3N2 Influenza A- Virus Switzerland 2013 Recombinant
Product # :
Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Full-Length H3N2 Switzerland 2013 is glycosylated with N-linked sugars, produced using baculovirus vectors in insect cells.
Source
Baculovirus Insect Cells.
Formulation
The Recombinant H3N2 A/ Switzerland 2013 solution contains 10mM Sodium phosphate, pH 7.1,150mM NaCl and 0.005% Tween-20.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
H3N2 is a subtype of the influenza A virus. Its name derives from the forms of the two kinds of proteinson the surface of its coat, hemagglutinin(H) and neuraminidase(N). H3N2 exchanges genes for internal proteins with other influenza subtypes. H3N2 has tended to dominate in prevalence over H1N1, H1N2, and influenza B. H3N2 strain descended from H2N2 by antigenic shift, in which genes from multiple subtypes re-assorted to form a new virus. Both the H2N2and H3N2 strains contained genesfrom avian influenzaviruses.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
H3N2 A/ Switzerland 2013 recombinant should be stored at 4°C. Do not freeze!
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LILRB1 HumanDescription:
Leukocyte Immunoglobulin Like Receptor B1 Human Recombinant
Leukocyte immunoglobulin-like receptor subfamily B member 1,Leukocyte immunoglobulin-like receptor 1, leucocyte Ig-like receptor B1, CD85 antigen-like family member J, Immunoglobulin-like transcript 2, myeloid inhibitory receptor 7, Monocyte/macrophage immunoglobulin-like receptor 7, Ig-like transcript 2, MIR-7, LILRB1, ILT2, LIR1, MIR7, LIR-1, ILT-2, PIRB, PIR-B
Product # :
PRO-2668Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LILRB1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 446 amino acids (24-461 a.a) and having a molecular mass of 48.5kDa.LILRB1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The LILRB1 solution (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Biological activity is > 50%. It is defined by the ability of the immobilized protein to support the adhesion of HSB2 human peripheral blood acute lymphoblastic leukemia cells, while the cells are added to LILRB1 coated plates at 5ug/ml.
More Info
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Introduction
Leukocyte Immunoglobulin Like Receptor B1 (LILRB1) is a member of the leukocyteimmunoglobulinlike receptor (LIR) family. LILRB1is expressed on immune cells, binds to MHC classI molecules on antigen-presenting cells and transduces a negative signal that inhibits stimulation of an immuneresponse. LILRB1 controls inflammatory responses and cytotoxicity to help focus the immune responseand limit autoreactivity. LILRB1 is also expressed on the surface of B cells and monocytes, subsets of NKcells, gamma δ T cells,memory/effector CD8+ T cells and monocyte-derived dendritic cells.
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Synonyms
Leukocyte immunoglobulin-like receptor subfamily B member 1,
Leukocyte immunoglobulin-like receptor 1, leucocyte Ig-like receptor B1, CD85 antigen-like family member J, Immunoglobulin-like transcript 2, myeloid inhibitory receptor 7, Monocyte/macrophage immunoglobulin-like receptor 7, Ig-like transcript 2, MIR-7, LILRB1, ILT2, LIR1, MIR7, LIR-1, ILT-2, PIRB, PIR-B -
Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
GHLPKPTLWA EPGSVITQGS PVTLRCQGGQ ETQEYRLYRE KKTAPWITRI PQELVKKGQF PIPSITWEHT GRYRCYYGSD TAGRSESSDP LELVVTGAYI KPTLSAQPSP VVNSGGNVTL QCDSQVAFDG FILCKEGEDE HPQCLNSQPH ARGSSRAIFS VGPVSPSRRW WYRCYAYDSN SPYEWSLPSD LLELLVLGVS KKPSLSVQPG PIVAPEETLT LQCGSDAGYN RFVLYKDGER DFLQLAGAQP QAGLSQANFT LGPVSRSYGG QYRCYGAHNL SSEWSAPSDP LDILIAGQFY DRVSLSVQPG PTVASGENVT LLCQSQGWMQ TFLLTKEGAA DDPWRLRSTY QSQKYQAEFP MGPVTSAHAG TYRCYGSQSS KPYLLTHPSD PLELVVSGPS GGPSSPTTGP TSTSGPEDQP LTPTGSDPQS GLGRHLGVLE HHHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Kisspeptin-10Description:
Kisspeptin-10
Product # :
HOR-044Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Kisspeptin-10 Synthetic is a single, non-glycosylated polypeptide chain containing 10 amino acids, having a molecular mass of 1302 Dalton and a Molecular formula of C63H83N17O14 .
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Kisspeptin-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Kisspeptin-10 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Kisspeptin-10 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
H-Tyr-Asn-Trp-Asn-Ser-Phe-Gly-Leu-Arg-Phe-NH2.
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Background
Kisspeptin-10, a peptide derived from the Kisspeptin gene (KISS1), has emerged as a key player in the regulation of reproductive physiology. The peptide is known for its potent ability to stimulate the release of gonadotropin-releasing hormone (GnRH), a crucial factor in the control of the hypothalamic-pituitary-gonadal axis. The pivotal role of kisspeptin-10 in orchestrating the onset of puberty and the regulation of the menstrual cycle highlights its significance in reproductive health. This research aims to delve into the multifaceted functions of kisspeptin-10, shedding light on its physiological roles and potential applications in reproductive disorders.
The primary objective of this study is to comprehensively explore the effects of kisspeptin-10 on the reproductive system. In vitro and in vivo assays will be conducted to investigate the impact of kisspeptin-10 on GnRH release and subsequent gonadotropin secretion. The interactions between kisspeptin-10 and its receptor, G protein-coupled receptor 54 (GPR54), will be explored using binding assays, potentially unraveling novel signaling pathways activated by this interaction.
The second objective is to investigate the potential therapeutic applications of kisspeptin-10 in reproductive disorders. Clinical studies and animal models will be utilized to assess the efficacy of kisspeptin-10 in stimulating ovulation, particularly in cases of infertility caused by hypothalamic dysfunction. Furthermore, the potential of kisspeptin-10 in regulating conditions like polycystic ovary syndrome (PCOS) and hypogonadotropic hypogonadism will be explored.
The third objective is to elucidate the molecular mechanisms underlying the actions of kisspeptin-10. Transcriptomic and proteomic analyses will be employed to identify genes and proteins regulated by kisspeptin-10 stimulation. This information could reveal novel downstream effectors of kisspeptin-10 signaling, contributing to a more comprehensive understanding of its role in reproductive physiology.
By delving into the complexities of kisspeptin-10, this research aims to provide insights into its multifunctional roles in reproductive health and expand its potential therapeutic applications. The findings from this study may pave the way for the development of targeted interventions for reproductive disorders, potentially improving the quality of life for individuals affected by these conditions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL 1 alpha HumanDescription:
Interleukin-1 alpha Human 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-253Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-1 alpha Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 159 amino acids and having a molecular mass of 18022 Dalton. 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 25mM Tris-HCl, pH 8.
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 < 0.001 ng/ml, corresponding to a Specific Activity of 1 x 109 IU/mg.More Info
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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 from synovial cells.
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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.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-1 alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1a should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interleukin 1 alpha in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SAPFSFLSNVKYNFMRIIKYEFILNDALNQSIIRANDQYLTAAALHNLDEAV KFDMGAYKSSKDDAKITVILRISKTQLYVTAQDEDQPVLLKEMPEIPKTITG SETNLLFFWETHGTKNYFTSVAHPNLFIATKQDYWVCLAGGPPSITDFQILE NQA.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.13 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-1 as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IFNG FelineDescription:
Interferon-gamma Feline Recombinant
Interferon gamma, IFN-gamma, IFNG.
Product # :
CYT-998Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- SDS-PAGE
Description
IFNG Feline Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 167 amino acids (24-167 a.a) and having a molecular mass of 19.3kDa.IFNG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IFNG protein solution (1mg/ml) containing PBS buffer (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
SDS-PAGE
More Info
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Introduction
IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons. -
Synonyms
Interferon gamma, IFN-gamma, IFNG.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQAMFFKE IEELKGYFNA SNPDVADGGS LFVDILKNWK EESDKTIIQS QIVSFYLKMF ENLKDDDQRI QRSMDTIKED MLDKLLNTSS SKRDDFLKLI QIPVNDLQVQ RKAINELFKV MNDLSPRSNL RKRKRSQNLF RGRRASK.
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Background
What is the molecular weight/Mw of IFNG FELINE Protein?
IFNG FELINE Protein has a total Mw of 19.3kDa.
What is the source or expression system of IFNG FELINE Protein?
Escherichia Coli.
What is the Purity of IFNG FELINE Protein?
IFNG FELINE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNG FELINE Protein?
The biological functionality of IFNG FELINE Protein will be determined in the future.
What is the amino acid sequence of IFNG FELINE Protein?
MGSSHHHHHH SSGLVPRGSH MGSQAMFFKE IEELKGYFNA SNPDVADGGS LFVDILKNWK EESDKTIIQS QIVSFYLKMF ENLKDDDQRI QRSMDTIKED MLDKLLNTSS SKRDDFLKLI QIPVNDLQVQ RKAINELFKV MNDLSPRSNL RKRKRSQNLF RGRRASK.
What applications can IFNG FELINE Protein be used in?
IFNG FELINE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNG FELINE Protein?
The endotoxin level is minimal, IFNG FELINE 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 :
il 18 HumanDescription:
Interleukin-18 Human Recombinant
IGIF, IL-1g, IL-18, IL1F4, MGC12320, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma, Iboctadekin.
Product # :
CYT-269Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-18 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 157 amino acids and having a molecular mass of 18.2 kDa. The IL-18 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.0.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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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.
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Synonyms
IGIF, IL-1g, IL-18, IL1F4, MGC12320, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma, Iboctadekin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin 18 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL18 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interleukin 18 in sterile PBS at 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
YFGKLESKLS VIRNLNDQVL FIDQGNRPLF EDMTDSDCRD NAPRTIFIIS MYKDSQPRGM AVTISVKCEK ISTLSCENKI ISFKEMNPPD NIKDTKSDII FFQRSVPGHD NKMQFESSSY EGYFLACEKE RDLFKLILKK EDELGDRSIM FTVQNED
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Background
Also known as IFN-gamma inducing factor, Interleukin-18 or IL18 is a protein. In humans this protein is encoded by the IL18 gene. The protein is a proinflammatory cytokine.
Mechanism
The levels of IL-18 in the human body are increased at sites of inflammation. This includes cases of rheumatoid arthritis as well as other similar conditions. Osteoblastic cells express the protein and it is capable of inhibiting osteoclast formation. It is able to do this through a variety of mechanisms.
For instance, it is able to stimulate GM-CSF. This is created by T cells and is a response to treatment using IL-18. As well as this, the cytokine does stimulate INF-y production through vivo in bone. Furthermore, the impact on bone resorption and osteoclastogenesis is increased when used in conjunction with IL-12 treatment. Studies have shown that IL-18 provides an indirect stimulus on osteoclastogenesis due to the effect it has on T lymphocytes.
Furthermore, evidence has shown that IL-18 does increase the production of OPG. This was studied in research on transgenic mice that overexpressed IL-18. In these cases osteoclasts decreased as did bone mass. This suggested that IL-18 also has an impact on bone growth.
Interactions
Research has also explored the different interactions of IL-18 on other proteins. This includes the interaction between IL-18 and IL-18R. This has been shown to decrease the power of protective immunity and increase pathogenic responses during an infection involving intracellular bacteria. This interaction suggests that the presence or absence of IL-18R signal does impact the pathogenic compared to protective immunity.
Another interaction between interleukin 19 and Astrocyte has shown that it can improve neuropathic pain processing following nerve injury. It is proposed this is due to the fact that the nociceptive signals in the spinal cord are augmented due to this reaction.
Function
Belonging to the IL-1 superfamily, this cytokine is produced by macrophages as well as various other cells. It operates after binding with the interleukin-18 receptor. Working with IL-12, the protein is then able to induce-cell mediated immunity after an infection from lipopolysaccharide and other microbial products.
Once stimulated by IL-18 other cells including natural killer and T cells then release IFN-y. This type II IFN plays a crucial part in activating the macrophages of various other cells.
Together IL12 and IL-18 are able to successfully inhibit IgE and IG1 production that is dependent on IL-4. As well as this, the protein is also able to increase IgG2a production through B cells. IL-18 will interact specifically with this type of cytokine and has a negative impact on regulation of biological activity.
Structure
Many researchers have suggested that the structure of IL-18 is a key way to understand it’s receptor activation mechanism. The structure of IL-18 closely resembles of IL-1 and has various similarities. It is folded into a beta-trefoil structure and three sites have been shown to be important for receptor activation. These were revealed through extensive mutagenesis. Two of the sites provide binding sites for the IL-18 receptor and are located in positions similar to IL-1. The third structure seems to be used for IL-18 receptor beta binding.
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 :
RLN2 Human, Sf9Description:
Relaxin-2 Human Recombinant, Sf9
Relaxin 2, Relaxin, Ovarian, Of Pregnancy, Prorelaxin H2, Relaxin H2, H2-Preprorelaxin, Relaxin 2 (H2), BA12D24.1.1, BA12D24.1.2, H2-RLX, RLXH2, H2.
Product # :
PRO-2406Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RLN2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 170 amino acids (25-185a.a.) and having a molecular mass of 19.3kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).RLN2 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
RLN2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Prorelaxin H2 (RLN2) is a member of the insulin gene superfamily. This family which is produced by the ovary, targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. It may also have other roles in boosting sperm motility, regulating blood pressure, controlling heart rate and releasing oxytocin and vasopressin. RLN2 is a peptide hormone linked to several therapeutically relevant physiological effects, including regulation of collagen metabolism and multiple vascular control pathways. The active form of the RLN2 protein consists of an A chain and a B chain linked by disulfide bonds.
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Synonyms
Relaxin 2, Relaxin, Ovarian, Of Pregnancy, Prorelaxin H2, Relaxin H2, H2-Preprorelaxin, Relaxin 2 (H2), BA12D24.1.1, BA12D24.1.2, H2-RLX, RLXH2, H2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPDSWMEEV IKLCGRELVR AQIAICGMST WSKRSLSQED APQTPRPVAE IVPSFINKDT ETINMMSEFV ANLPQELKLT LSEMQPALPQ LQQHVPVLKD SSLLFEEFKK LIRNRQSEAA DSSPSELKYL GLDTHSRKKR QLYSALANKC CHVGCTKRSL ARFCHHHHHH.
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.