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1000 results found for “influenza”
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Name :
CXCL8 Human, GSTDescription:
Interleukin-8 (1-72) (CXCL8) Human Recombinant, GST Tag
Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8
Product # :
CHM-047Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human Interleukin-8 produced in E. coli containing 72 amino acids.Recombinant Human Interleukin-8 is fused to GST tag at its N-terminus and purified by proprietary chromatographic technique.
Source
Escherichia Coli.
Formulation
IL8 GST solution contains 25mM Tris-Base/ 25mM K2CO3.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
Citations
More Info
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Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
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Synonyms
Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Applications
Immunoassay.
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Background
What is the source or expression system of CXCL8 HUMAN, GST Protein?
Escherichia Coli.
What is the Purity of CXCL8 HUMAN, GST Protein?
CXCL8 HUMAN, GST Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL8 HUMAN, GST Protein?
The biological functionality of CXCL8 HUMAN, GST Protein will be determined in the future.
What is the amino acid sequence of CXCL8 HUMAN, GST Protein?
CXCL8 HUMAN, GST Protein is composed from 72 amino acids.
What applications can CXCL8 HUMAN, GST Protein be used in?
CXCL8 HUMAN, GST Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL8 HUMAN, GST Protein?
The endotoxin level is minimal, CXCL8 HUMAN, GST Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL8 HUMAN, GST that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CXCL8 HUMAN, GST?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
IL36A Mouse, HisDescription:
Interleukin-36 Alpha Mouse Recombinant, His Tag
Interleukin-36 alpha, FIL1 epsilon, Interleukin-1 epsilon, IL-1 epsilon, Interleukin-1 family member 6, IL-1F6, Interleukin-1 homolog 1, IL-1H1, Il36a, Fil1e, Il1e, Il1f6, Il1h1.
Product # :
CYT-905Price :
Quantity :
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Shipped with Ice Packs
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Description
IL36A Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (1-160 a.a) and having a molecular mass of 20.4kDa. IL36A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
IL36A protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Human IL-36a belongs to the IL-1 family which includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36ra (IL1F5), IL-36b (IL1F8), IL-36g (IL1F9), IL-37 (IL1F7) and IL-38 (IL-1F10). The IL-1 family members display a 12 b-strand, b-trefoil configuration, and are thought to have ascended from a mutual ancestral gene. IL-36a is an 18-22kDa, 158aa intracellular and secreted protein which holds no signal sequence, no prosegment and no potential from N-linked glycosylation sites. IL-36a is released as a reaction to LPS and the cell ATP-induced activation of the P2X7 receptor.
Human IL-36a (aa 6-158) shares 57-68% aa sequence homology with mouse, rabbit, equine and bovine IL-36a and 27-57% aa sequence homology with other new IL-1 family members. IL-36a is mostly found in skin and lymphoid tissues, but also in fetal brain, trachea, stomach and intestine. -
Synonyms
Interleukin-36 alpha, FIL1 epsilon, Interleukin-1 epsilon, IL-1 epsilon, Interleukin-1 family member 6, IL-1F6, Interleukin-1 homolog 1, IL-1H1, Il36a, Fil1e, Il1e, Il1f6, Il1h1.
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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 MGSMNKEKEL RAASPSLRHV QDLSSRVWIL QNNILTAVPR KEQTVPVTIT LLPCQYLDTL ETNRGDPTYM GVQRPMSCLF CTKDGEQPVL QLGEGNIMEM YNKKEPVKAS LFYHKKSGTT STFESAAFPG WFIAVCSKGS CPLILTQELG EIFITDFEMI VVH.
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 :
CCL24 HumanDescription:
Eotaxin-2 Human Recombinant (CCL24)
C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.
Product # :
CHM-238Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CCL24 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 78 amino acids and having a molecular mass of 8.8 kDa. The CCL24 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CCL24 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM PBS pH-7.4 and 0.15M sodium chloride.
Purity
Greater than 97.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is determined by the chemoattract of human PBE (peripheral blood eosinophils) at a concentration between 50-100 ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.Citations
More Info
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Introduction
Eotaxin-2, also called MPIF2 & Ckb6, is a novel CC chemokine produced by activated monocytes and T lymphocytes. Eotaxin-2 selectively chemoattracts cells expressing CCR3 including eosinophils, basophils, Th2 T cells, mast cells, and certain subsets of dendritic cells. Furthermore, Eotaxin-2 inhibits the proliferation of multipotential hematopoietic progenitor cells. The mature protein, which includes C-terminal truncation, contains 78 amino acids (92 amino acids for the mouse homolog, without C-terminal truncation).
CCL24 functions as a chemotactic chemokine for resting t-lymphocytes, and eosinophils. CCL24 has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. CCL24 is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line and binds to CCR3. -
Synonyms
C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Eotaxin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL24 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 CCL24 Human Recombinant 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
VVIPSPCCMFFVSKRIPENRVVSYQLSSRSTCLKGGVIFTTKKGQQFCG
DPKQEWV QRYMKNLDAKQKKASPRARAVA. -
Background
What is the molecular weight/Mw of CCL24 HUMAN Protein?
CCL24 HUMAN Protein has a total Mw of 8.8kDa.
What is the source or expression system of CCL24 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL24 HUMAN Protein?
CCL24 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL24 HUMAN Protein?
The activity is determined by the chemoattract of human PBE (peripheral blood eosinophils) at a concentration between 50-100 ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.
What is the amino acid sequence of CCL24 HUMAN Protein?
VVIPSPCCMFFVSKRIPENRVVSYQLSSRSTCLKGGVIFTTKKGQQFCG
DPKQEWV QRYMKNLDAKQKKASPRARAVA.
What applications can CCL24 HUMAN Protein be used in?
CCL24 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL24 HUMAN Protein?
The endotoxin level is minimal, CCL24 HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant CCL24 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CCL24 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
IL16 Human, HisDescription:
Interleukin-16 Human Recombinant, His Tag
IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.
Product # :
CYT-562Price :
Quantity :
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Shipped with Ice Packs
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Description
Interleukin-16 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain (502-631 a.a) containing 150 amino acids and having a molecular mass of 15.5kDa. The IL-16 is fused to a 20 a.a His-Tag at N-Terminus.The IL-16 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL-16 His tag protein (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM PMSF & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
SDS-PAGE
Citations
More Info
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Introduction
IL-16 is a pleiotropic cytokine that functions as a chemoattractant, a modulator of T cell activation, and an inhibitor of HIV replication. The signaling process of IL-16 is mediated by CD4. The product of this gene undergoes proteolytic processing, which is found to yield two functional proteins. IL-16 functions exclusively attributed to the secreted C-terminal peptide, while the N-terminal product may play a role in cell cycle control. Caspase 3 is reported to be involved in the proteolytic processing of this protein. Two transcript variants encoding different isoforms have been found for this gene.
IL-16 stimulates a migratory response in cd4+ lymphocytes, monocytes, and eosinophils. Also induces t-lymphocyte expression of interleukin 2 receptor, ligand for cd4. -
Synonyms
IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.
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Physical Appearance
Sterile Filtered solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPDLNSSTDS AASASAASDV SVESTAEATV CTVTLEKMSAGLGFSLEGGK GSLHGDKPLT INRIFKGAAS EQSETVQPGD EILQLGGTAM QGLTRFEAWN IIKALPDGPV TIVIRRKSLQ SKETTAAGDS.
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Background
What is the molecular weight/Mw of IL16 HUMAN, HIS Protein?
IL16 HUMAN, HIS Protein has a total Mw of 15.5kDa.
What is the source or expression system of IL16 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of IL16 HUMAN, HIS Protein?
IL16 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IL16 HUMAN, HIS Protein?
The biological functionality of IL16 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of IL16 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MPDLNSSTDS AASASAASDV SVESTAEATV CTVTLEKMSAGLGFSLEGGK GSLHGDKPLT INRIFKGAAS EQSETVQPGD EILQLGGTAM QGLTRFEAWN IIKALPDGPV TIVIRRKSLQ SKETTAAGDS.
What applications can IL16 HUMAN, HIS Protein be used in?
IL16 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL16 HUMAN, HIS Protein?
The endotoxin level is minimal, IL16 HUMAN, HIS Protein was purified using conventional chromatography techniques.
Who supplies recombinant IL16 HUMAN, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of IL16 HUMAN, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
BPIFA1 HumanDescription:
BPI fold containing family A Member 1 Human Recombinant
BPI fold-containing family A member 1, Lung-specific protein X, Nasopharyngeal carcinoma-related protein, Palate lung and nasal epithelium clone protein, Secretory protein in upper respiratory tracts, Tracheal epithelium-enriched protein, Von Ebner protein Hl, BPIFA1, LUNX, NASG, PLUNC, SPURT, SPLUNC1, bA49G10.5.
Product # :
PRO-404Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
BPIFA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 260 amino acids (20-256 a.a) and having a molecular mass of 27.1kDa.BPIFA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BPIFA1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl and 30% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
BPI fold containing family A Member 1 (BPIFA1) belongs to the short subfamily of PLUNC family proteins and have homology only to the Nterminal domains of BPI. BPIFA1 is a secreted protein which is expressed in the secretory ducts and submucosal glands of tracheobronchial tissues. BPIFA1 binds to LPS (lipopolysaccharide) in nasal lavage fluid (NLF) which alludes to its role in the inflammatory response of the upper airways after exposure to irritants. BPIFA1 may also serve as a potential molecular marker for detection of micrometastasis in non-small-cell lung cancer. Decreased levels of BPIFA1 are observed in the NLF of smokers and people who have been exposed to reactive epoxy chemicals, which indicats that long-term exposure to airway irritants damages the production of BPIFA1 in the upper respiratory tract.
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Synonyms
BPI fold-containing family A member 1, Lung-specific protein X, Nasopharyngeal carcinoma-related protein, Palate lung and nasal epithelium clone protein, Secretory protein in upper respiratory tracts, Tracheal epithelium-enriched protein, Von Ebner protein Hl, BPIFA1, LUNX, NASG, PLUNC, SPURT, SPLUNC1, bA49G10.5.
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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 MGSQFGGLPV PLDQTLPLNV NPALPLSPTG LAGSLTNALS NGLLSGGLLG ILENLPLLDI LKPGGGTSGG LLGGLLGKVT SVIPGLNNII DIKVTDPQLL ELGLVQSPDG HRLYVTIPLG IKLQVNTPLV GASLLRLAVK LDITAEILAV RDKQERIHLV LGDCTHSPGS LQISLLDGLG PLPIQGLLDS LTGILNKVLP ELVQGNVCPL VNEVLRGLDI TLVHDIVNML IHGLQFVIKV.
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 :
hCG HumanDescription:
Chorionic Gonadotropin Human
Chorionic gonadotropin, hCG, CG.
Product # :
HOR-250Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Chorionic Gonadotropin is produced from a sterile preparation of placental glucoprotein urine of pregnant women having a total molecular mass of 36,700 Dalton. The hCG consists of 237 amino acids, a chain-92 amino acids and b chain-145 amino acids. The hCG is purified by proprietary chromatographic techniques.
Source
Urine of pregnant women.
Formulation
The hCG was lyophilized with no additives.
Biological Activity
The activity was found to be 5238IU/mg.
Activity Assay
Citations
More Info
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Introduction
Human chorionic gonadotropin (hCG) is a peptide hormone produced in pregnancy, that is made by the embryosoon after conception and later by the syncytiotrophoblast(part of the placenta). Its role is to prevent the disintegration of the corpus luteumof the ovaryand thereby maintain progesterone production that is critical for a pregnancy in humans. hCG may have additional functions, for instance it is thought that it affects the immune tolerance of the pregnancy. Early pregnancy testing generally is based on the detection or measurement of hCG.
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Synonyms
Chorionic gonadotropin, hCG, CG.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized hCG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CG-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 Human Chorionic Gonadotropin 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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Background
What is the molecular weight/Mw of HCG HUMAN Protein?
HCG HUMAN Protein has a total Mw of 36.7kDa.
What is the source or expression system of HCG HUMAN Protein?
Urine of pregnant women.
What is the Biological Activity of HCG HUMAN Protein?
The activity was found to be 5238IU/mg.
What is the amino acid sequence of HCG HUMAN Protein?
HCG HUMAN Protein is composed from 237 amino acids.
What applications can HCG HUMAN Protein be used in?
HCG HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for HCG HUMAN Protein?
The endotoxin level is minimal, HCG HUMAN Protein was purified using conventional chromatography techniques.
Who supplies HCG HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of HCG HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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Contaminants
Free of: HbsAg and antibodies to HIV and HCV.
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 :
TNFRSF14 Human, HisDescription:
HVEM Human Recombinant, His Tag
Tumor Necrosis Factor Receptor Superfamily Member 14, HVEM, TR2, Herpes Virus Entry Mediator A, Tumor Necrosis Factor Receptor-Like 2, Herpesvirus Entry Mediator, HVEA, ATAR, CD270, LIGHTR, CD40-Like Protein, Tumor Necrosis Factor Receptor-Like Gene2.
Product # :
CYT-800Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TNFRSF14 Human Recombinant produced in E. Coli is a single, glycosylated polypeptide chain containing 187 amino acids (39-202) and having a molecular mass of 19.7kDa.TNFRSF14 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TNFRSF14 solution (0.5mg/ml) containing 20mM Tris-HCl (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TNFRSF14, a member of the TNF receptor superfamily, is a type I transmembrane protein. TNFRSF14 is expressed in peripheral blood T cells, B cells, monocytes and in various tissues enriched in lymphoid cells. TNFRSF14 operates as a co-stimulatory factor for the activation of lymphoid cells and as a deterrent to infection by herpesvirus. Additionally, TNFRSF14 encourages the proliferation of T cells, and triggers apoptosis of various tumor cells.
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Synonyms
Tumor Necrosis Factor Receptor Superfamily Member 14, HVEM, TR2, Herpes Virus Entry Mediator A, Tumor Necrosis Factor Receptor-Like 2, Herpesvirus Entry Mediator, HVEA, ATAR, CD270, LIGHTR, CD40-Like Protein, Tumor Necrosis Factor Receptor-Like Gene2.
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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 MGSLPSCKED EYPVGSECCP KCSPGYRVKE ACGELTGTVC EPCPPGTYIA HLNGLSKCLQ CQMCDPAMGL RASRNCSRTE NAVCGCSPGH FCIVQDGDHC AACRAYATSS PGQRVQKGGT ESQDTLCQNC PPGTFSPNGT LEECQHQTKC SWLVTKAGAG TSSSHWV.
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 :
Bartonella 26kDaDescription:
Bartonella Henselae 26kDa Recombinant
Product # :
PRO-2569Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Bartonella Henselae 26kDa produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 25kDa. Bartonella 26kDa is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Bartonella 26kDa is supplied at a 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% Glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Numerous forms of Bartonellosis are caused by Bartonella henselae as well as Cat Scratch Disease & Bacillary Angiomatosis. It has been found that up to 95% of patients with Cat Scratch Disease show antibodies against Bartonella henselae antigens.
Highly immunoreactive proteins which are produced by the Bartonella henselae are the most important antigens used for the diagnosis of Cat Scratch Disease.
Bartonella henselae of outer membrane protein p26 has an important nucleotide identity with orthologs in Bartonella spp, Brucella spp in addition to more than a few plant-associated bacteria.
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Physical Appearance
Sterile Filtered solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
HSPA9 HumanDescription:
Heat Shock 70kDa Protein 9 Human Recombinant
Mortalin, GRP75, MOT2, GSPA9B, PBP74, MOT-2, MTHSP75, Stress-70 protein mitochondrial, 75 kDa glucose-regulated protein, GRP 75, Heat shock 70 kDa protein 9, Peptide-binding protein 74, MOT, HSPA9, HSPA9B, CSA, MGC4500.
Product # :
HSP-023Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human HSPA9 produced in E.Coli is a single,non-glycosylated polypeptide chain containing 654 amino acids (47-679) and having a molecular mass of 71 kDa.HSP9A is expressed with a 20 amino acid His tag fused at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HSPA9 protein solution contains 20mM Tris-HCl, pH-8, 10% glycerol and 0.5mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HSPA9 is part of the heat shock protein 70 family which contains both heat-inducible and constitutively expressed members that are also called heat-shock cognate proteins. HSPA9 encodes a heat-shock cognate protein that is involved in the control of cell proliferation and acts as a chaperone. HSPA9 was restricted to chromosome 5, band q31, a region that is often deleted in myeloid leukemias and myelodysplasia (MDS), making it a candidate tumor suppressor gene, which is consistent with the biological function of its murine homologue. HSPA9 supresses nuclear translocation, transcriptional activation, and control of centrosome-duplication functions of p53.
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Synonyms
Mortalin, GRP75, MOT2, GSPA9B, PBP74, MOT-2, MTHSP75, Stress-70 protein mitochondrial, 75 kDa glucose-regulated protein, GRP 75, Heat shock 70 kDa protein 9, Peptide-binding protein 74, MOT, HSPA9, HSPA9B, CSA, MGC4500.
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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 MASEAIKGAV VGIDLGTTNS CVAVMEGKQA KVLENAEGAR TTPSVVAFTA DGERLVGMPA KRQAVTNPNN TFYATKRLIG RRYDDPEVQK DIKNVPFKIV RASNGDAWVE AHGKLYSPSQ IGAFVLMKMK ETAENYLGHT AKNAVITVPA YFNDSQRQAT KDAGQISGLN VLRVINEPTA AALAYGLDKS EDKVIAVYDL GGGTFDISIL EIQKGVFEVK STNGDTFLGG EDFDQALLRH IVKEFKRETG VDLTKDNMAL QRVREAAEKA KCELSSSVQT DINLPYLTMD SSGPKHLNMK LTRAQFEGIV TDLIRRTIAP CQKAMQDAEV SKSDIGEVIL VGGMTRMPKV QQTVQDLFGR APSKAVNPDE AVAIGAAIQG GVLAGDVTDV LLLDVTPLSL GIETLGGVFT KLINRNTTIP TKKSQVFSTA ADGQTQVEIK VCQGEREMAG DNKLLGQFTL IGIPPAPRGV PQIEVTFDID ANGIVHVSAK DKGTGREQQI VIQSSGGLSK DDIENMVKNA EKYAEEDRRK KERVEAVNMA EGIIHDTETK MEEFKDQLPA DECNKLKEEI SKMRELLARK DSETGENIRQ AASSLQQASL KLFEMAYKKM ASEREGSGSS GTGEQKEDQK EEKQ.
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 :
EREG Human, HEKDescription:
Epiregulin Human Recombinant, HEK
EPR, Epiregulin, Ep, ER, Proepiregulin, EREG.
Product # :
CYT-1206Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EREG Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (63-108a.a) containing 289 amino acids and having a molecular mass of 32.6 kDa.EREG is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
EREG protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 1ug/ml.
Citations
More Info
-
Introduction
"Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence."
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Synonyms
EPR, Epiregulin, Ep, ER, Proepiregulin, EREG.
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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
DGSMVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH
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Background
What is the molecular weight/Mw of EREG Protein?
EREG Protein has a total Mw of 32.6kDa.
What is the source or expression system of EREG Protein?
HEK293 cells.
What is the Purity of EREG Protein?
EREG Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of EREG Protein?
Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 1ug/ml.
What is the amino acid sequence of EREG Protein?
DGSMVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH
What applications can EREG Protein be used in?
EREG Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EREG Protein?
The endotoxin level is minimal, EREG 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 :
KLRF1 HumanDescription:
Killer Cell lectin-like Receptor Subfamily F Member 1 Human Recombinant
NKp80, KLRF1, C-type lectin domain family 5 member C, CLEC5C, ML, Killer cell lectin-like receptor F1, Killer cell lectin-like receptor subfamily F member 1,Killer cell lectin-like receptor subfamily F member 1 isoform 1, Lectin-like receptor F1, Activating coreceptor NKp80, CLEC5CMGC119908, MGC119907, MGC119909.
Product # :
PRO-2753Price :
Quantity :
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Shipped with Ice Packs
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Description
KLRF1 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 414 amino acids (60-231a.a) and having a molecular mass of 47.1kDa.KLRF1 is fused to a 242 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The KLRF1 solution (0.25mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Biological Activity
Measured by the ability of the immobilized protein to support the adhesion of U937 human histiocytic lymphoma cells. When cells are added to human KLRF1 coated plates 2 ug/ml. This effect is more to 60%.
Citations
More Info
-
Introduction
Killer cell lectin-like receptor subfamily F member 1, aka KLRF1, is a member of the C-type lectin family. KLRF1, an activating homodimeric C-type lectin-like receptor (CTLR), is expressed on nearly all natural killer (NK) cells and stimulates their cytoxicity and cytokine release. Killer cell lectin-like receptor subfamily F member 1 works through interaction with its ligand, AICL (activation-induced C-type lectin), which is selectively expressed on myeloid cells. AICL interaction regulates the immune responses at sites of inflammation by stimulating the release of proinflammatory cytokines. Diseases associated with KLRF1 include Developmental And Epileptic Encephalopathy 76.
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Synonyms
NKp80, KLRF1, C-type lectin domain family 5 member C, CLEC5C, ML, Killer cell lectin-like receptor F1, Killer cell lectin-like receptor subfamily F member 1,Killer cell lectin-like receptor subfamily F member 1 isoform 1, Lectin-like receptor F1, Activating coreceptor NKp80, CLEC5CMGC119908, MGC119907, MGC119909.
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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.
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Amino Acid Sequence
DGSLLVSQGV LLKCQKGSCS NATQYEDTGD LKVNNGTRRN ISNKDLCASR SADQTVLCQS EWLKYQGKCY WFSNEMKSWS DSYVYCLERK SHLLIIHDQL EMAFIQKNLR QLNYVWIGLN FTSLKMTWTW VDGSPIDSKI FFIKGPAKEN SCAAIKESKI FSETCSSVFK WICQYLEPKS CDRTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH 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 :
Borrelia Afzelii OspCDescription:
Borrelia Afzelii Outer Surface Protein C Recombinant
Product # :
BOR-016Price :
Quantity :
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Shipped with Ice Packs
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Description
Recombinant Borrelia Afzelii Outer Surface Protein C produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 22,151 Dalton. Borrelia Afzelii OspC is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Borrelia Afzelii OspC is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG- and IgM-type human antibodies.2. Immunodot test with Lyme disease positive/negative plasma.
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 :
FLRT3 HumanDescription:
Fibronectin Leucine Rich Transmembrane Protein 3 Human Recombinant
Fibronectin Leucine Rich Transmembrane Protein 3, Fibronectin-Like Domain, Containing Leucine-Rich Transmembrane Protein 3, HH21, Leucine-Rich Repeat, Transmembrane Protein FLRT3, KIAA1469.
Product # :
PRO-2181Price :
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Description
FLRT3 produced in Sf9 insect cells is a single, glycosylated polypeptide chain containing 508 amino acids (29-528a.a.) and having a molecular mass of 57.6kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).FLRT3 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
FLRT3 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Fibronectin Leucine Rich Transmembrane Protein 3, also known as FLRT3 is a member of the fibronectin leucine rich transmembrane protein (FLRT) family. FLRT3 contains one fibronectin type-III domain as well as 10 LRR (leucine-rich) repeats and is expressed in the kidney, brain, pancreas, skeletal muscle, lung, liver, placenta, and heart. In addition, the members of the FLRT family play a role in cell adhesion as well as receptor signaling. FLRT3 has been implicated in neurite outgrowth after nerve damage, as a positive regulator of FGF signalling and in homotypic cell adhesion. Furthermore, FLRT3 has an essential function in regulating cellular adhesion among the epithelial apical ridge and the underlying mesenchyme and also in the establishment of the dorso-ventral position of the ridge.
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Synonyms
Fibronectin Leucine Rich Transmembrane Protein 3, Fibronectin-Like Domain, Containing Leucine-Rich Transmembrane Protein 3, HH21, Leucine-Rich Repeat, Transmembrane Protein FLRT3, KIAA1469.
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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
KSCPSVCRCD AGFIYCNDRF LTSIPTGIPE DATTLYLQNN QINNAGIPSD LKNLLKVERI YLYHNSLDEF PTNLPKYVKE LHLQENNIRT ITYDSLSKIP YLEELHLDDN SVSAVSIEEG AFRDSNYLRL LFLSRNHLST IPWGLPRTIE ELRLDDNRIS TISSPSLQGL TSLKRLVLDG NLLNNHGLGD KVFFNLVNLT ELSLVRNSLT AAPVNLPGTN LRKLYLQDNH INRVPPNAFS YLRQLYRLDM SNNNLSNLPQ GIFDDLDNIT QLILRNNPWY CGCKMKWVRD WLQSLPVKVN VRGLMCQAPE KVRGMAIKDL NAELFDCKDS GIVSTIQITT AIPNTVYPAQ GQWPAPVTKQ PDIKNPKLTK DHQTTGSPSR KTITITVKSV TSDTIHISWK LALPMTALRL SWLKLGHSPA FGSITETIVT GERSEYLVTA LEPDSPYKVC MVPMETSNLY LFDETPVCIE TETAPLRMYN PTTTLNREQE KEPYKNPNLP LEHHHHHH.
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 :
BLyS Human, HisDescription:
B cell Activating Factor Human Recombinant, His Tag
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.
Product # :
CYT-545Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
BLyS Human Recombinant fused to His tag at N-terminus produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (134-285 a.a.) and having a molecular mass of 21 kDa. BAFF is fused to a 38 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Recombinant His Tag BAFF contains PBS pH-7.4 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
sds-page
Citations
More Info
-
Introduction
Binds to tnfrsf13b/taci and tnfrsf17/bcma. tnfsf13/april binds to the same 2 receptors, together, they form a 2 ligands -2 receptors pathway involved in the stimulation of b- and t-cell function and the regulation of humoral immunity. a third b-cell specific baff-receptor (baffr/br3) promotes the survival of mature b-cells and the b-cell response.
B Lymphocyte Stimulator functions as a potent B-cell growth factor in costimulation assays.
Administration of BAFF Human recombinant to mice disrupts splenic B-cell and T-cell zones and results in elevated levels of serum immunoglobulin. -
Synonyms
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.
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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.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMAV QGPEETVTQD CLQLIADSET PTIQKGSYTF VPWLLSFKRG SALEEKENKI LVKETGYFFI YGQVLYTDKT YAMGHLIQRK KVHVFGDELS LVTLFRCIQN MPETLPNNSC YSAGIAKLEE GDELQLAIPR ENAQISLDGD VTFFGALKLL
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Background
What is the molecular weight/Mw of BLYS Protein?
BLYS Protein has a total Mw of 21kDa.
What is the source or expression system of BLYS Protein?
Escherichia Coli.
What is the Purity of BLYS Protein?
BLYS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BLYS Protein?
The biological functionality of BLYS Protein will be determined in the future.
What is the amino acid sequence of BLYS Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMAV QGPEETVTQD CLQLIADSET PTIQKGSYTF VPWLLSFKRG SALEEKENKI LVKETGYFFI YGQVLYTDKT YAMGHLIQRK KVHVFGDELS LVTLFRCIQN MPETLPNNSC YSAGIAKLEE GDELQLAIPR ENAQISLDGD VTFFGALKLL
What applications can BLYS Protein be used in?
BLYS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BLYS Protein?
The endotoxin level is minimal, BLYS 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 :
IL12B AntibodyDescription:
Interleukin-12 subunit beta, Mouse Anti Human
Interleukin-12 subunit beta, IL-12 subunit p40, Cytotoxic lymphocyte maturation factor 40 kDa subunit, NK cell stimulatory factor chain 2, IL-12B, CLMF p40, NKSF2, IL12B, CLMF, CLMF2, IL-12B.
Product # :
ANT-435Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- More Info
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Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
Citations
More Info
-
Introduction
IL12B is a subunit of interleukin 12 which is a cytokine that acts on T and natural killer cells, and has a broad array of biological activities. Interleukin 12 is a disulfide-linked heterodimer composed of the 40kDa cytokine receptor like subunit encoded by the IL12B gene, and a 35kDa subunit encoded by IL12A. The IL12B cytokine is expressed by activated macrophages which serve as an important inducer of Th1 cells development. The IL12B cytokine has been found to be important for sustaining a sufficient number of memory/effector Th1 cells to mediate long-term protection to an intracellular pathogen. Overexpression of the IL12B gene was observed in the central nervous system of patients with multiple sclerosis (MS), suggesting a role of the IL12B cytokine in the pathogenesis of the disease. The promoter polymorphism of the IL12B gene has been reported to be linked to the severity of atopic and non-atopic asthma in children.
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Synonyms
Interleukin-12 subunit beta, IL-12 subunit p40, Cytotoxic lymphocyte maturation factor 40 kDa subunit, NK cell stimulatory factor chain 2, IL-12B, CLMF p40, NKSF2, IL12B, CLMF, CLMF2, IL-12B.
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Physical Appearance
Sterile Filtered clear solution.
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Immunogen
Anti-human IL12B mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human IL12B amino acids 23-328 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
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Clone
PAT1D6AT.
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Applications
IL12B antibody has been tested by ELISA and 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 dilution range for Western blot analysis is 1:1000 ~ 2000. 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
IL12B antibody was purified from mouse ascitic fluids by protein-G 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 :
PDCD6IP HumanDescription:
Programmed Cell Death 6 Interacting Protein Human Recombinant
AIP1, Alix, PDCD6-Interacting Protein, DRIP4, ALG-2 interacting protein 1, Programmed cell death 6-interacting protein, Hp95, PDCD6IP, KIAA1375, MGC17003.
Product # :
PRO-792Price :
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Description
PDCD6IP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 412 amino acids (1-392 a.a.) and having a molecular mass of 45.8 kDa. The PDCD6IP is fused to a 20 amino acid His-tag at N-terminus and purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
PDCD6IP is a Class E VPS protein which participates in concentration and sorting of cargo proteins of the multivesicular body or incorporation into intralumenal vesicles that are generated by invagination and scission from the limiting membrane of the endosome. PDCD6IP binds to the phospholipid lysobisphosphatidic acid which is abundant in MVBs internal membranes. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. PDCD6IP is an adapter for a subset of ESCRT-III proteins, such as CHMP4, to function at distinct membranes. PDCD6IP is mandatory for completion of cytokinesis. PDCD6IP takes part in HIV-1 virus budding. PDCD6IP replaces TSG101 in its function of supporting HIV-1 release. PDCD6IP takes part in the regulation of both apoptosis and cell proliferation. PDCD6IP is a cytoplasmic protein that cooperates with apoptosis-associated proteins (ALG-2 and PDCD6) and with the endocytosis-regulator CIN85. Overexpression of PDCD6IP and endophilin
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Synonyms
AIP1, Alix, PDCD6-Interacting Protein, DRIP4, ALG-2 interacting protein 1, Programmed cell death 6-interacting protein, Hp95, PDCD6IP, KIAA1375, MGC17003.
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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 MATFISVQLK KTSEVDLAKP LVKFIQQTYP SGGEEQAQYC RAAEELSKLR RAAVGRPLDK HEGALETLLR YYDQICSIEP KFPFSENQIC LTFTWKDAFD KGSLFGGSVK LALASLGYEK SCVLFNCAAL ASQIAAEQNL DNDEGLKIAA KHYQFASGAF LHIKETVLSA LSREPTVDIS PDTVGTLSLI MLAQAQEVFF LKATRDKMKD AIIAKLANQA ADYFGDAFKQ CQYKDTLPKE VFPVLAAKHC IMQANAEYHQ SILAKQQKKF GEEIARLQHA AELIKTVASR YDEYVNVKDF SDKINRALAA AKKDNDFIYH DRVPDLKDLD PIGKATLVKS TPVNVPISQK FTDLFEKMVP VSVQQSLAAY NQRKADLVNR SIAQMREATT LA.
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 :
FertirelinDescription:
Fertirelin
Product # :
HOR-037Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Fertirelin Synthetic is a single, non-glycosylated polypeptide chain containing 9 amino acids, having a molecular mass of 1153.31 Dalton and a Molecular formula of C55H76N16O12.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
Citations
More Info
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Fertirelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fertirelin 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 Fertirelin 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
Pyr-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-NHEt.
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Background
Fertirelin, a potent gonadotropin-releasing hormone (GnRH) analogue, is crucial for fertility regulation in animals. This research paper endeavors to expound on the biochemical attributes of fertirelin and its potential therapeutic applications in veterinary medicine.
Fertirelin, a synthetic analogue of the natural gonadotropin-releasing hormone, plays a fundamental role in fertility regulation in veterinary medicine. It stimulates the secretion of luteinizing hormone and follicle-stimulating hormone, crucial for reproduction (Kotwica et al., 2005). This paper aims to delve into the biochemical characteristics of fertirelin and its potential applications.
Fertirelin, as a GnRH analogue, elicits its action by binding to GnRH receptors located on pituitary gonadotroph cells. This leads to the release of luteinizing hormone and follicle-stimulating hormone, key players in ovulation and spermatogenesis (Kotwica et al., 2005).
In the realm of veterinary medicine, fertirelin is primarily used for treating ovarian follicular cysts in dairy cattle (Bosu & Peter, 1987). Its potent stimulatory effect on gonadotropin secretion facilitates ovulation and contributes to fertility management strategies.
The potential of fertirelin extends beyond the current applications. Further research into the precise mechanism of action and potential side effects can enhance its utilization. Overall, fertirelin presents a powerful tool in veterinary reproductive medicine, making it a focal point of interest for future studies.
What is the molecular weight/Mw of FERTIRELIN Protein?
FERTIRELIN Protein has a total Mw of 1.15kDa.
What is the Purity of FERTIRELIN Protein?
FERTIRELIN Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of FERTIRELIN Protein?
The biological functionality of FERTIRELIN Protein will be determined in the future.
What is the amino acid sequence of FERTIRELIN Protein?
Pyr-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-NHEt.
What applications can FERTIRELIN Protein be used in?
FERTIRELIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FERTIRELIN Protein?
The endotoxin level is minimal, FERTIRELIN Protein was purified using conventional chromatography techniques.
Who supplies FERTIRELIN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of FERTIRELIN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
HIV-1 nefDescription:
HIV-1 nef Recombinant
Product # :
HIV-124Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
The E.coli derived 20kDa recombinant protein genotype IIIB is a non-glycosylated polypeptide chain, containing the HIV-1 nef immunodominant regions, 3-190 amino acids. The HIV-1 nef is fused to beta-galactosidase (114 kDa) at the N-terminus.
Source
Escherichia Coli.
Formulation
HIV-1 nef protein solution in 8M urea, 20mM Tris-HCl pH 8.0, 10mM b-mercaptoethanol.
Purity
Greater than 95.0% as determined by HPLC analysis and SDS-PAGE.
Citations
More Info
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Introduction
Human immunodeficiency virus (HIV) is a retrovirus that can lead to a condition in which the immune system begins to fail, leading to opportunistic infections. HIV primarily infects vital cells in the human immune system such as helper T cells (specifically CD4+ T cells), macrophages and dendritic cells. HIV infection leads to low levels of CD4+ T cells through three main mechanisms: firstly, direct viral killing of infected cells; secondly, increased rates of apoptosis in infected cells; and thirdly, killing of infected CD4+ T cells by CD8 cytotoxic lymphocytes that recognize infected cells. When CD4+ T cell numbers decline below a critical level, cell-mediated immunity is lost, and the body becomes progressively more susceptible to opportunistic infections. HIV was classified as a member of the genus Lentivirus, part of the family of Retroviridae. Lentiviruses have many common morphologies and biological properties. Many species are infected by lentiviruses, which are characteristically responsible for long-duration illnesses with a long incubation period. Lentiviruses are transmitted as single-stranded, positive-sense, enveloped RNA viruses. Upon entry of the target cell, the viral RNA genome is converted to double-stranded DNA by a virally encoded reverse transcriptase that is present in the virus particle. This viral DNA is then integrated into the cellular DNA by a virally encoded integrase so that the genome can be transcribed. Once the virus has infected the cell, two pathways are possible: either the virus becomes latent and the infected cell continues to function, or the virus becomes active and replicates, and a large number of virus particles are liberated that can then infect other cells.
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Physical Appearance
Sterile filtered colorless clear solution.
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Stability
HIV-1 nef although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
kwskssv igwptvrerm rraepaadgv gaasqdlekh gaitssntaa tnadcawlea
qeeeevgfpv tpqvplrpmt ykaavdlshf lkekgglegl ihsqrrqdil dlwiyhtqgy
fpdwqnytpg pgirypltfg wcyklvpvep ekleeankge ntsllhpvsl hgmddperev
lewrfdsrla.
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 :
T.gondii MIC-3Description:
Toxoplasma Gondii MIC 3 Recombinant
Product # :
TOX-261Price :
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Description
The E.Coli derived recombinant protein contains the MIC3 immunodominant regions, amino acids 234-306. MIC3 protein is fused to a 26Kda Glutathione transferase tag.
Source
Escherichia Coli.
Formulation
50mM Tris-HCl pH 8.0, 1mM EDTA and 8M urea.
Purity
Toxoplasma protein is >95% pure as determined by 10% PAGE (coomassie staining).
Citations
More Info
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Introduction
The life cycle of Toxoplasma gondii has two phases. The coccidia like takes place only in members of the Felidae family which makes these animals the parasite's primary host. The asexual part of the life cycle can take place in any warm-blooded animal, like other mammals(including felines) and birds. T. gondii constructing daughter scaffolds within the mother cell. In the intermediate hosts (including felines), the parasite invades cells, forming intracellular so-called parasitophorous vacuoles containing bradyzoites, the slowly replicating form of the parasit. Vacuoles form tissue cysts mainly within the muscles and brain. Since they are within cells, the host's immune system does not detect these cysts. Resistance to antibiotics varies, but the cysts are very difficult to eradicate entirely. Within these vacuoles T. gondii propagates by a series of binary fissions until the infected cell eventually bursts and tachyzoites are released. Tachyzoites are the motile, asexually reproducing form of the parasite. Unlike the bradyzoites, the free tachyzoites are usually efficiently cleared by the host's immune response, although some manage to infect cells and form bradyzoites, thus maintaining the infection.
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Stability
Toxoplasma protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
Toxoplasma antigen is suitable in ELISA and Western blots, excellent antigen for detection of Toxoplasma gondii- with minimal specificity problems.
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Specificity
Immunoreactive with sera of Toxoplasma gondii-infected individuals.
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Purification Method
Toxoplasama protein was purified by GS-4B Sepharose-Affinity Purification.
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 :
LIF Human, YeastDescription:
LIF Human Recombinant, Yeast
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
Product # :
CYT-191Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
LIF Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 180 amino acids and having a molecular mass of 58.5 kDa. The LIF is purified by proprietary chromatographic techniques.
Source
Pichia pastoris.
Formulation
The protein was lyophilized from a 0.2 µm filtered PBS.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity of recombinant human LIF was measured by the ability to induce differentiation of murine M1 myeloid leukemic cells. The minimal detectable concentration of human LIF in this assay is <0.05 ng/mL. The specific activity is > 1 x 108 units/mg.Citations
More Info
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Introduction
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
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Synonyms
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized LIF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LIF 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 LIF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
S P L P I T P V N A T C A I R H P C H N N L M N Q I R S Q L A Q L N G S A N A L F I L Y Y T A Q G E P F P N N L D K L C G P N V T D F P P F H A N G T E K A K L V E L Y R I V V Y L G T S L G N I T R D Q K I L N P S A L S L H S K L N A T A D I L R G L L S N V L C R L C S K Y H V G H V D V T Y G P D T S G K D V F Q K K K L G C Q L L G K Y K Q I I A V L A Q A F.
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.
Citations
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 :
T.pallidum p41 MosaicDescription:
Treponema pallidum p41 Mosaic Recombinant
Product # :
TRP-244Price :
Quantity :
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Shipped with Ice Packs
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Description
The E.coli derived recombinant protein contains the outer membrane T.Pallidum p41 immunodominant regions. The protein is fused with a GST tag.
Source
Escherichia Coli.
Formulation
25mM Tris-HCl pH-8, 60mM NaCl & 50% glycerol.
Purity
Treponema Pallidum protein is >90% pure as determined by 10% PAGE (coomassie staining).
Citations
More Info
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Introduction
Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum sub sp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.
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Stability
Treponema Pallidum protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
Treponema Pallidum protein is suitable for ELISA and Western blots, excellent antigen for detection of T. Pallidum with minimal specificity problems.
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Specificity
Immunoreactive with sera of T.Pallidum infected individuals.
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Purification Method
Treponema Pallidum protein was purified by proprietary chromatographic technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GHRLDescription:
Ghrelin Human
Appetite-regulating hormone precursor, Growth hormone secretagogue, Growth hormone-releasing peptide, GHRP, Motilin-related peptide, M46 protein, Ghrelin, Obestatin, MTLRP.
Product # :
HOR-297Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Ghrelin Human contains 28 amino acids and a total molecular mass of 3370.9 Dalton and a molecular formula of C149H249N47O42.The GHRL is purified by proprietary chromatographic techniques.
Formulation
GHRL was lyophilized without additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Citations
More Info
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Introduction
Obestatin is a hormone that is produced in the cells lining the stomach and small intestine of several mammals including humans; it drastically reduces appetite in mice and is expected to do the same in humans. Obestatin is a peptide hormone - a relatively small protein. It is encoded by the same gene that also encodes ghrelin, a peptide hormone that increases appetite. The protein produced by that gene breaks into two smaller peptides, ghrelin and obestatin. Ghrelin is an endogenous ligand for the growth hormone secretagogue receptor and is involved in regulating growth hormone release. Ghrelin is derived from a preprohormone called preproghrelin, which also generates a second peptide called obestatin. Ghrelin is an endogenous ligand for the orphan G protein-coupled receptor GPR39 and is involved in satiety and decreased food intake.
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Synonyms
Appetite-regulating hormone precursor, Growth hormone secretagogue, Growth hormone-releasing peptide, GHRP, Motilin-related peptide, M46 protein, Ghrelin, Obestatin, MTLRP.
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Physical Appearance
Sterile Filtered Yellowish lyophilized (freeze-dried) powder that may appear as a gel form.
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Stability
Store the lyophilized Ghrelin at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted GHRL can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
Add deionized water to a working concentration approximately 0.5mg/1ml and let the lyophilized pellet dissolve completely.
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Amino Acid Sequence
Gly-Ser-Ser(n-octanoyl)-Phe-Leu-Ser-Pro-Glu-His-Gln-Arg-Val-Gln-Gln-Arg-Lys-Glu-Ser-Lys-Lys-Pro-Pro-Ala-Lys-Leu-Gln-Pro-Arg-OH.
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Background
What is the molecular weight/Mw of GHRL Protein?
GHRL Protein has a total Mw of 3.37kDa.
What is the Purity of GHRL Protein?
GHRL Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of GHRL Protein?
The biological functionality of GHRL Protein will be determined in the future.
What is the amino acid sequence of GHRL Protein?
Gly-Ser-Ser(n-octanoyl)-Phe-Leu-Ser-Pro-Glu-His-Gln-Arg-Val-Gln-Gln-Arg-Lys-Glu-Ser-Lys-Lys-Pro-Pro-Ala-Lys-Leu-Gln-Pro-Arg-OH.
What applications can GHRL Protein be used in?
GHRL Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GHRL Protein?
The endotoxin level is minimal, GHRL Protein was purified using conventional chromatography techniques.
Who supplies GHRL that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of GHRL?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
IL6 Rat, sf9Description:
Interleukin-6 Rat Recombinant, sf9
IL6, Ifnb2, ILg6.
Product # :
CYT-1048Price :
Quantity :
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Shipped with Ice Packs
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Description
IL6 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 196 amino acids (25-211 a.a.) and having a molecular mass of 22.8kDa (Molecular size on SDS-PAGE will appear at approximately 18-28 kDa).IL6 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IL6 protein solution (0.5mg/ml) contains 20% glycerol & Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using M-NFS-60 mouse B cell. The ED50 for this effects is less or equal to 0.1 ng/ml.
Citations
More Info
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Introduction
Interleukin-6 is a potent pro-inflammatory cytokine primarily produced by activated T cells and an assortment of other cells including endothelial cells and macrophages. IL-6 affects B and T lymphocytes and has been shown to have a role in host defense, acute phase reactions, immune responses and hematopoiesis.
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Synonyms
IL6, Ifnb2, ILg6.
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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
ADPFPTSQVR RGDFTEDTTH NRPVYTTSQV GGLITYVLRE ILEMRKELCN GNSDCMNSDDALSENNLKLP EIQRNDGCFQ TGYNQEICLL KICSGLLEFR FYLEFVKNNL QDNKKDKARVIQSNTETLVH IFKQEIKDSY KIVLPTPTSN ALLMEKLESQ KEWLRTKTIQ LILKALEEFL KVTMRSTRQT HHHHHH
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Background
Production and Applications of Rat Recombinant Interleukin-6 in sf9 Cells
Abstract:
Interleukin-6 (IL-6) is a critical cytokine involved in various physiological processes, including inflammation, immune responses, and hematopoiesis. The production of recombinant IL-6 has paved the way for numerous applications in research and therapeutic development. This paper elucidates the production of Rat Recombinant IL-6 in sf9 cells using baculovirus expression system and explores its potential applications in immunology and disease research.
Introduction:
Interleukin-6 is a pleiotropic cytokine with diverse functions in immune regulation, acute phase responses, and tissue homeostasis. The ability to produce recombinant IL-6 allows researchers to investigate its role in various biological contexts and develop potential therapies. The sf9 cell line, derived from Spodoptera frugiperda insect cells, offers an efficient platform for recombinant protein expression through the baculovirus system.
Methods:
The production of Rat Recombinant IL-6 involves inserting the rat IL-6 gene into a baculovirus transfer vector. This vector is then co-transfected with a linearized baculovirus DNA into sf9 cells. The resulting recombinant baculovirus expresses the IL-6 protein, which is secreted into the culture medium. The expressed protein is subsequently purified using chromatographic techniques to ensure its quality and activity.
Applications:
Rat Recombinant IL-6 produced in sf9 cells has widespread applications. It serves as a valuable tool for investigating the mechanisms underlying IL-6-mediated immune responses, inflammation, and hematopoiesis. Furthermore, it enables the development of potential therapies targeting IL-6-related disorders, including autoimmune diseases, inflammatory conditions, and certain types of cancer.
Advantages of sf9 Expression:
The sf9 expression system offers several advantages, including high protein yields, post-translational modifications, and proper protein folding. This system is especially suitable for complex cytokines like IL-6, which require correct tertiary structure for optimal biological activity.
Challenges and Future Prospects:
While sf9-based expression of Rat Recombinant IL-6 offers numerous benefits, challenges such as optimization of expression conditions, scale-up, and quality control remain. Additionally, further research is needed to explore the therapeutic potential of Rat Recombinant IL-6 in preclinical and clinical settings.
Conclusion:
The production of Rat Recombinant IL-6 in sf9 cells using the baculovirus expression system provides a powerful tool for unraveling the roles of IL-6 in various biological processes. This platform holds promise for advancing our understanding of IL-6-related diseases and facilitating the development of targeted therapeutic interventions.
What is the molecular weight/Mw of IL6 RAT, SF9 Protein?
IL6 RAT, SF9 Protein has a total Mw of 22.8kDa.
What is the source or expression system of IL6 RAT, SF9 Protein?
Sf9, Baculovirus cells.
What is the Purity of IL6 RAT, SF9 Protein?
IL6 RAT, SF9 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IL6 RAT, SF9 Protein?
Measured in a cell proliferation assay using M-NFS-60 mouse B cell. The ED50 for this effects is less or equal to 0.1 ng/ml.
What is the amino acid sequence of IL6 RAT, SF9 Protein?
ADPFPTSQVR RGDFTEDTTH NRPVYTTSQV GGLITYVLRE ILEMRKELCN GNSDCMNSDDALSENNLKLP EIQRNDGCFQ TGYNQEICLL KICSGLLEFR FYLEFVKNNL QDNKKDKARVIQSNTETLVH IFKQEIKDSY KIVLPTPTSN ALLMEKLESQ KEWLRTKTIQ LILKALEEFL KVTMRSTRQT HHHHHH.
What applications can IL6 RAT, SF9 Protein be used in?
IL6 RAT, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL6 RAT, SF9 Protein?
The endotoxin level is minimal, IL6 RAT, SF9 Protein was purified using conventional chromatography techniques.
Who supplies recombinant IL6 RAT, SF9 that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of IL6 RAT, SF9?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets
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.