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Name :
Leptin Human, MutantDescription:
Leptin Mutant D23L Human Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1243Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Leptin Mutant D23L is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus and having a molecular mass of ~ 16 kDa. Leptin Mutant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
Leptin Mutant was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Human Leptin Mutant D23L is fully biologically active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.
More Info
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Human Leptin Mutant D23L although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Mutant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids of recombinant human leptin was determined and was found to be Ala-Val-Pro-Ile-Gln.
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Background
Leptin’s main part is to regulate long-term energy balance. Leptin is a hormone which mainly produced by adipocytes and is encoded by the LEP gene. Leptin effects mainly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor is found on a wide range of cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
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 :
Betacellulin HumanDescription:
Betacellulin Human Recombinant
Product # :
CYT-330Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Betacellulin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 80 amino acids and having a molecular mass of 9 kDa. Betacellulin Human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Betacellulin Human Recombinant was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50, calculated by the dose-dependant proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 0.05 ng/ml. corresponding to a Specific Activity of >20,000,000IU/mg.More Info
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Introduction
Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Betacellulin Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BTC Human 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 BTC Human 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
DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY
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Background
Betacellulin Human Recombinant: Illuminating Pathways in Regenerative Medicine
Introduction
In the ever-evolving landscape of regenerative medicine, a promising new chapter unfolds with the arrival of Betacellulin Human Recombinant (BTC). This growth factor holds tremendous potential, offering a glimpse into the future of transformative therapeutic interventions.
BTC: The Architect of Cellular Revitalization
BTC, a member of the EGF family, has long been recognized for its pivotal role in cellular proliferation and differentiation. The emergence of BTC in its recombinant form has sparked excitement, igniting new possibilities for regenerative medicine.
Crafting the Alchemist: Pioneering Methodologies
Through the adept utilization of biotechnological techniques, we successfully synthesized BTC human recombinant. Our meticulous in vitro investigations delved into BTC's capacity to orchestrate intricate cellular processes, paving the way for therapeutic advancements.
Unveiling the Biological Tapestry
Buoyed by encouraging in vitro findings, we embarked on in vivo studies utilizing animal models. This natural setting allowed us to witness BTC human recombinant's impact within a living organism, unraveling the intricate nuances of its regenerative potential.
A Flourish of Results
The journey from laboratory to living system yielded promising results. BTC human recombinant showcased a significant influence on cellular proliferation and differentiation, underscoring its role as a key player in tissue regeneration and regenerative therapies.
Charting a Transformative Future
As the story of BTC human recombinant unfolds, it beckons further exploration through extensive human-centric clinical trials. These trials will serve as a compass, guiding us towards harnessing the full therapeutic potential of BTC, ushering in a new era of healing and regeneration.
What is the molecular weight/Mw of BTC Protein?
BTC Protein has a total Mw of 9kDa.
What is the source or expression system of BTC Protein?
Escherichia Coli.
What is the Purity of BTC Protein?
BTC Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of BTC Protein?
The ED50, calculated by the dose-dependant proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 0.05 ng/ml. corresponding to a Specific Activity of >20,000,000IU/mg.
What is the amino acid sequence of BTC Protein?
DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY
What applications can BTC Protein be used in?
BTC Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BTC Protein?
The endotoxin level is minimal, BTC 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 :
Acrp30 AntibodyDescription:
Adiponectin, Mouse Anti Human
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
ANT-232Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Formulation
containing PBS, pH-7.4, & 0.1% Sodium Azide
More Info
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Introduction
Human Adiponectin is a secreted protein expressed exclusively in differentiated adipocyte (adipokine). Adiponectin contains a modular structure comprising an N-terminal collagenous domain followed by a C-terminal globular domain. APM-1 plays a role in various physiological processes such as energy homeostasis and obesity. Plasma levels of adiponectin are reduced in obese humans, and decreased levels are associated with insulin resistance and hyperinsulinemia.
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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Physical Appearance
Sterile Filtered solution.
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Immunogen
Anti-human adiponectin mAb, is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human adiponectin amino acids 15-244 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and k light chain.
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Clone
P1G12AT.
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Applications
Adiponectin antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Recommended dilution range for Western blot analysis is 1:250 ~ 1:1,000. The antibody has the specificity against globular domain of adiponectin. Recommended starting dilution is 1:500.
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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
Adiponectin 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.
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Name :
Cadherin-E HumanDescription:
Cadherin-E Human Recombinant
Epithelial cadherin, E-cadherin, Uvomorulin, Cadherin-1, CAM 120/80, CD324 antigen, CDH1, CDHE, UVO, ECAD, LCAM, Arc-1, CD324, Cadherin-E.
Product # :
PRO-461Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Cadherin-E Human Recombinant (aa 600-707) expressed in E.coli, shows a 38 kDa band on SDS-PAGE.The Cadherin-E is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Cadherin-E protein (100µg/1ml) in 50mM Tris-HCl, pH7.5 and 10mM L-glutathione (reduced).
More Info
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Introduction
E-cadherin (uvomorulin, cell-CAM120/80) is a calcium dependent cell adhesion molecule expressed predominately in epithelial tissues. It plays an important role in the growth and development of cells via the mechanisms of control of tissue architecture and the maintenance of tissue integrity. Numerous studies have demonstrated that reduction and/or loss of Ecadherin expression in carcinomas correlates positively with the potential of these tumors for invasion and metastasis.
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Synonyms
Epithelial cadherin, E-cadherin, Uvomorulin, Cadherin-1, CAM 120/80, CD324 antigen, CDH1, CDHE, UVO, ECAD, LCAM, Arc-1, CD324, Cadherin-E.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.
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Amino Acid Sequence
iffcernpkpq viniidadlp pntspftael thgasanwti qyndptqesi ilkpkmalev gdykinlklm dnqnkdqvtt levsvcdceg aagvcrkaqp veaglqi.
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 :
CKMB Human ActiveDescription:
Creatine Kinase MB Active Human Recombinant
CKMB, CK-MB
Product # :
CKI-200Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CKMB Human Recombinant produced in E. coli is a noncovalently-linked heterodimer consists of CK-M and CK-B each containing 381 amino acids and having a total molecular mass of 85.7kDa (43.10 kDa and 42.64 kDa respectively). CKMB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was Lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris and 150mM NaCl, pH 8.0.
Purity
Greater than 95.0% as determined by Analysis by SDS-PAGE.
Biological Activity
The specific activity ranges from 500-600 units/mg and was measured kinetically by the CK-NAC assay at 37°C.More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CKMB Active although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CKMB Active should be stored at 4°C between 2-7 days and for future use below -18°C.
Please prevent freeze-thaw cycles. -
Solubility
It is recommended to reconstitute the lyophilized CKMB 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
CKM
MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG FTVDDVIQTG VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EKEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV LTCPSNLGTG LRGGVHVKLA HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ K
CKB
MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K.
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Background
CKMB is used in cardiovascular research as a biomarker for myocardial injury and to investigate the molecular mechanisms of cardiac muscle damage and repair.
CKMB is also used in Immunoassay development, Aptamer screening, Biosensor validation and Point-of-care diagnostic assay development
What is the molecular weight / Mw of CKMB Protein?
CKMB Protein is a non covalently heterodimer having a total Mw of 85.7ka
What is the source or expression system of CKMB Protein?
Escherichia Coli.
What is the Purity of CKMB Protein?
CKMB Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CKMB Protein?
The activity was determined kinetically by the CK-NAC assay at 37°C which ranges between 500-600 U/mg.
What is the amino acid sequence of CKMB Protein?
CKM
MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG FTVDDVIQTG VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EKEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV LTCPSNLGTG LRGGVHVKLA HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ K
CKB
MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K
What applications can CKMB Protein be used in?
CKMB Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CKMB Protein?
The endotoxin level is minimal, CKMB 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 :
CDH5 MouseDescription:
Cadherin 5 Mouse Recombinant
Cadherin-5, Vascular endothelial cadherin, VE-cadherin, CD144, Cdh5.
Product # :
PRO-2244Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CDH5 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 583 amino acids (25-599a.a.) and having a molecular mass of 66.2kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).CDH5 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
CDH5 protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cadherin-5, also known as CDH5 is a classical cadherin which belongs to the cadherin superfamily. The CDH5is located in a six-cadherin cluster in a region on the long arm of chromosome 16 which is involved in loss ofheterozygosity events in breast as well as prostate cancer. CDH5 is a calcium-dependent cell-celladhesion glycoprotein composed of five extracellular cadherin repeats, a transmembrane region and a highlyconserved cytoplasmic tail. Furthermore, CDH5 functions as a classic cadherin by passing on to cells the ability to adhere in ahomophilic manner, CDH5 plays a significant role in endothelial cell biology through control of the cohesion as well as organization of the intercellular junctions.
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Synonyms
Cadherin-5, Vascular endothelial cadherin, VE-cadherin, CD144, Cdh5.
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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
GPNFPQIDTP NMLPAHHRQK RDWIWNQMHI DEEKNESLPH YVGKIKSNVN RQNAKYVLQG EFAGKIFGVD ANTGNVLAYE RLDREKVSEY FLTALIVDKN TNKNLEQPSS FTVKVHDIND NWPVFSHQVF NASVPEMSAI GTSVIRVTAV DADDPTVAGH ATVLYQIVKG NEYFSIDNSG LIFTKIKNLD REKQAEYKIV VETQDALGLR GESGTATVMI RLEDINDNFP VFTQSTYTFS VPEDIRVGKP LGFLTVVDPD EPQNRMTKYS IMQGEYRDTF TIETDPKRNE GIIKPTKSLD YEVIQQYTFY IEATDPTIRY EYLSSTSGKN KAMVTINVLD VDEPPVFQRH FYHFKLPENQ KKPLIGTVVA KDPDKAQRSI GYSIRKTSDR GQFFRITKQG NIYNEKELDR ETYAWYNLTV EANELDSRGN PVGKESIVQV YIEVLDENDN PPEFAQPYEP KVCENAAQGK LVVQISATDK DVVPVNPKFK FALKNEDSNF TLINNHDNTA NITVKYGQFN REHAKFHYLP VLISDNGVPS LTGTSTLTVG VCKCNEQGEF TFCEEMAAQA GVSIQLEHHH HHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CCN1 HumanDescription:
Cysteine-Rich Angiogenic Inducer 61 Human Recombinant
CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.
Product # :
CYT-164Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
CYR61 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 357 amino acids and having a molecular mass of 39.5kDa.The CYR61 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2m filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 was determined by the proliferation of mouse 3T3 cells is < 2.0 ug/ml, corresponding to a specific activity of > 500 units/mg.More Info
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Introduction
CYR61 is a growth factor-inducible, immediate-early gene that has multifaceted activities in various cancers. CYR61 is a secreted, cysteine-rich, binding protein which is encoded by a growth factor-inducible immediate-early gene. Acting as an extracellular, matrix-associated signaling molecule, CYR61 promotes the adhesion of endothelial cells through interaction with integrin and enhances growth factor-induced DNA synthesis in the same cell type.
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Synonyms
CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CYR61 Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CYR61 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 CYR61 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
TCPAACHCPL EAPKCAPGVG LVRDGCGCCK VCAKQLNEDC SKTQPCDHTK GLECNFGASS TALKGICRAQ SEGRPCEYNS RIYQNGESFQ PNCKHQCTCI DGAVGCIPLC PQELSLPNLG CPNPRLVKVT GQCCEEWVCD EDSIKDPMED QDGLLGKELG FDASEVELTR NNELIAVGKG SSLKRLPVFG MEPRILYNPL QGQKCIVQTT SWSQCSKTCG TGISTRVTND NPECRLVKET RICEVRPCGQ PVYSSLKKGK KCSKTKKSPE PVRFTYAGCL SVKKYRPKYC GSCVDGRCCT
PQLTRTVKMR FRCEDGETFS KNVMMIQSCK CNYNCPHANE AAFPFYRLFN DIHKFRD -
Background
Title: Cysteine-Rich Angiogenic Inducer 61 Human Recombinant: A Potential Regulator of Angiogenesis
Abstract:
Cysteine-rich angiogenic inducer 61 (CYR61) is an important extracellular matrix-associated protein that plays a significant role in angiogenesis and cell adhesion. This research paper provides a comprehensive analysis of human recombinant CYR61, focusing on its production, characterization, and potential applications in regulating angiogenesis. The paper discusses the significance of CYR61 in physiological and pathological angiogenesis, including wound healing, tumor development, and cardiovascular diseases. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant CYR61 in various pathological conditions. The information presented in this paper aims to enhance our understanding of human recombinant CYR61 and its utility as a research tool and a potential regulator of angiogenesis.Introduction:
Cysteine-rich angiogenic inducer 61 (CYR61) is an extracellular matrix-associated protein that plays a crucial role in angiogenesis, the formation of new blood vessels from pre-existing ones. Human recombinant CYR61, produced through genetic engineering techniques, provides researchers with a valuable tool to study its biological functions and explore its therapeutic potential.Production and Characterization:
Recombinant CYR61 is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CYR61.Role in Angiogenesis:
CYR61 is involved in various aspects of angiogenesis, including endothelial cell proliferation, migration, and tube formation. It interacts with integrins and other cell surface receptors to modulate signaling pathways involved in angiogenic processes. Recombinant CYR61 serves as a valuable tool for studying the mechanisms underlying angiogenesis and exploring its potential as a therapeutic target.Therapeutic Implications:
The dysregulation of angiogenesis is associated with several pathological conditions, including cancer, cardiovascular diseases, and chronic wounds. Recombinant CYR61 has shown promise as a potential regulator of angiogenesis and a therapeutic agent. It can be used to promote or inhibit angiogenesis, depending on the specific context. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant CYR61 in various diseases, including cancer and ischemic disorders.Conclusion:
Human recombinant CYR61 is a valuable research tool and a potential regulator of angiogenesis. Its production, characterization, and applications in modulating angiogenic processes contribute to our understanding of angiogenesis and the development of novel therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant CYR61 offer promising prospects for improving outcomes in cancer, cardiovascular diseases, and wound healing.What is the molecular weight/Mw of CCN1 Protein?
CCN1 Protein has a total Mw of 39.5kDa.
What is the source or expression system of CCN1 Protein?
Escherichia Coli.
What is the Purity of CCN1 Protein?
CCN1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CCN1 Protein?
The ED50 was determined by the proliferation of mouse 3T3 cells is < 2.0 ug/ml, corresponding to a specific activity of > 500 units/mg.
What is the amino acid sequence of CCN1 Protein?
TCPAACHCPL EAPKCAPGVG LVRDGCGCCK VCAKQLNEDC SKTQPCDHTK GLECNFGASS TALKGICRAQ SEGRPCEYNS RIYQNGESFQ PNCKHQCTCI DGAVGCIPLC PQELSLPNLG CPNPRLVKVT GQCCEEWVCD EDSIKDPMED QDGLLGKELG FDASEVELTR NNELIAVGKG SSLKRLPVFG MEPRILYNPL QGQKCIVQTT SWSQCSKTCG TGISTRVTND NPECRLVKET RICEVRPCGQ PVYSSLKKGK KCSKTKKSPE PVRFTYAGCL SVKKYRPKYC GSCVDGRCCT
PQLTRTVKMR FRCEDGETFS KNVMMIQSCK CNYNCPHANE AAFPFYRLFN DIHKFRD
What applications can CCN1 Protein be used in?
CCN1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCN1 Protein?
The endotoxin level is minimal, CCN1 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 :
UPK3A HumanDescription:
Uroplakin 3A Human Recombinant
Uroplakin 3A, UPK3, UPIII, Uroplakin III, UP3A.
Product # :
PRO-988Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
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Description
UPK3A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 214 amino acids (19-207 a.a.) and having a molecular mass of 23.1kDa.UPK3A is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
UPK3A protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 150mM NaCl, 2mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
UPK3A is a member of the uroplakin-3 family. Uroplakins (UP) which are transmembrane proteins are important components of the urothelium that pass the lipid bilayer once (UPII, UPIIIa, and UPIIIb) or four times (UPIa and UPIb; both members of the "tetraspanin" family). All hold great luminal/extracellular domains, but only UPIIIa and UPIIIb have significant cytoplasmic shares in their C-termini. UPK3A is an extremely specific and moderately sensitive immunohistochemical marker for primary and metastatic urothelial carcinomas. Alterations in this gene are related to renal adysplasia.
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Synonyms
Uroplakin 3A, UPK3, UPIII, Uroplakin III, UP3A.
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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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMVNLQP QLASVTFATN NPTLTTVALE KPLCMFDSKE ALTGTHEVYL YVLVDSAISR NASVQDSTNT PLGSTFLQTE GGRTGPYKAV AFDLIPCSDL PSLDAIGDVS KASQILNAYL VRVGANGTCL WDPNFQGLCN PPLSAATEYR FKYVLVNMST GLVEDQTLWS DPIRTNQLTP YSTIDTWPGR RSGG.
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 :
Cyclophilin F Rat BioactiveDescription:
Cyclophilin-F Rat Recombinant Bioactive
Peptidyl-prolyl cis-trans isomerase F, mitochondrial, PPIase F, Cyclophilin D, CyP-D, CypD, Cyclophilin F, Rotamase F.
Product # :
ENZ-1019Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Cyclophilin F Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids (30-206 a.a) and having a molecular mass of 21.2Da. Cyclophilin F is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Cyclophilin F protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 1,300 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmol of suc-AAFP-PNA per minute at 37C in Tris–HCl pH 8.0 using chymotrypsin.More Info
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Introduction
PPIF is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIF accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIF is key component of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.
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Synonyms
Peptidyl-prolyl cis-trans isomerase F, mitochondrial, PPIase F, Cyclophilin D, CyP-D, CypD, Cyclophilin F, Rotamase F.
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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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSCSDGGAR GANSSSQNPL VYLDVGADGQ PLGRVVLELK ADVVPKTAEN FRALCTGEKG FGYKGSTFHR VIPAFMCQAG DFTNHNGTGG KSIYGSRFPD ENFTLKHVGP GVLSMANAGP NTNGSQFFIC TIKTDWLDGK HVVFGHVKEG MDVVKKIESF GSKSGKTSKK IVITDCGQLS.
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 :
MIF Human, ActiveDescription:
Macrophage Migration Inhibitory Factor Human Recombinant (Active)
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
Product # :
CYT-596Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
MIF human Recombinant was cloned into an E.coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques.Macrophage Inducing Factor Human Recombinant is a single, non-glycosylated, polypeptide chain containing 115 amino acids and having a molecular mass of 12.5 kDa.
Source
Escherichia Coli.
Formulation
MIF-Protein was lyophilized from 10mM sodium phosphate buffer pH-7.5.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Human PBMCs were cultured with 0 to 1000ng/ml Human MIF. Production of IL-8 was measured via ELISA after 24 hours. The ED50 which was found to be 88-132ng/ml.More Info
-
Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
-
Synonyms
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized MIF-protein although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIF-protein should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized MIF-Protein in sterile 18MΩ-cm H2O at a concentration between 0.1mg-1mg per 1ml.
-
Amino Acid Sequence
MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLM
AFGGSSEPCALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVY
INYYDMNAANVGWNNSTFA.
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 :
Ara h 8.0101Description:
Allergen Ara h 8.0101 Recombinant
Ara h 8 allergen.
Product # :
ALR-010Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Ara h 8.0101 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 18,192 Dalton. Ara h 8.0101 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
Ara h 8.0101 is supplied in 20mM HEPES buffer pH-8, 0.1M NaCl and 6M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
-
Introduction
Ara h 8.0101 which is a part of the PR-10 protein family is a Bet v 1-homologous panallergen. Ara h 8.0101 is cross-reactive with Gly m 4 from soy bean and Bet v 1 from silver birch. Ara h 8.0101 is responsible for oral allergy syndrome and also has low stability to roasting and no stability to gastric digestion.
-
Synonyms
Ara h 8 allergen.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
MALD3Description:
Non-Specific Lipid-Transfer Protein Mal d 3 Recombinant
Non-specific lipid-transfer protein, LTP, MALD3.
Product # :
ALR-023Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
- More Info
Description
Recombinant Non-Specific Lipid-Transfer Protein Mal d 3 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 12kDa.MALD3 is expressed with a 6xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
MALD3 is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
-
Introduction
MALD3 (a non-specific lipid transfer protein) is a major apple allergen. LTPs are found mainly in aerial plant organs such as leaves, seeds, flowers, and fruit. MALD3 is a heat-stable protein which is characterized by having resistance to pepsin hydrolysis.
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Synonyms
Non-specific lipid-transfer protein, LTP, MALD3.
-
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.Avoid multiple freeze-thaw cycles.
-
Immunological Functions
1. Binds IgE-type human antibodies.2. Immunodot test with positive/negative samples
-
Applications
Tested by LAL (Limulus Amoebocyte Lysate) chromogenic endotoxin assay.
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 :
CCL15 HumanDescription:
Macrophage Inflammatory Protein-5 Human Recombinant (CCL15)
Small inducible cytokine A15 precursor, CCL15, Macrophage inflammatory protein 5, MIP-5, MIP5, Chemokine CC-2, HCC-2, NCC-3, MIP- 1 delta, Leukotactin-1, LKN-1, Mrp-2b, C-C motif chemokine 15.
Product # :
CHM-230Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Macrophage Inflammatory Protein-5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 92 amino acids and having a molecular mass of 10.1 kDa. The MIP5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MIP5 was lyophilized from a concentrated (1mg/ml) solution containing 20mM PBS pH-7.4 and 100mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human T-lymphocytes using a concentration range of 1-10 ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.More Info
-
Introduction
CCL15, a new human CC chemokine, was isolated from a human fetal spleen cDNA library. CCL15 cDNA encodes a predicted 113 amino acid (aa) protein containing a putative signal peptide of 21 amino acids that is cleaved to generate a 92 aa residue mature protein. Within the CC family members, human CCL15 shares 45%, 44%, 35%, and 30% aa homology with mouse C10, human MPIF-1, human HCC-1, and mouse MIP-1?, respectively. The gene for MIP-5 is found on chromosome 17 where the genes for most of the human CC chemokines are located. Human CCL15 is expressed in T and B lymphocytes, NK cells, monocytes and monocyte-derived dendritic cells. Human MIP-5 is chemotactic for T cells and monocytes and has been shown to induce calcium flux in human CCR-1-transfected cells.
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Synonyms
Small inducible cytokine A15 precursor, CCL15, Macrophage inflammatory protein 5, MIP-5, MIP5, Chemokine CC-2, HCC-2, NCC-3, MIP- 1 delta, Leukotactin-1, LKN-1, Mrp-2b, C-C motif chemokine 15.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized MIP-5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL15 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized MIP5 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
QFINDAETELMMSKLPLENPVVLNSFHFAADCCTSYISQSIPCSLMKSYFETSSECSKP GVIFLTKKGRQVCAKPSGPGVQDCMKKLKPYSI.
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Background
What is the molecular weight/Mw of CCL15 HUMAN Protein?
CCL15 HUMAN Protein has a total Mw of 10.1kDa.
What is the source or expression system of CCL15 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL15 HUMAN Protein?
CCL15 HUMAN Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL15 HUMAN Protein?
Determined by its ability to chemoattract human T-lymphocytes using a concentration range of 1-10 ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of CCL15 HUMAN Protein?
QFINDAETELMMSKLPLENPVVLNSFHFAADCCTSYISQSIPCSLMKSYFETSSECSKP GVIFLTKKGRQVCAKPSGPGVQDCMKKLKPYSI.
What applications can CCL15 HUMAN Protein be used in?
CCL15 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL15 HUMAN Protein?
The endotoxin level is minimal, CCL15 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
BD 4 RatDescription:
BD 4 Rat
Beta-defensin 4, BD-4, BD-2, Defensin, beta 4, RBD-2, RBD-4, Defb4, Defb2, Defb3.
Product # :
CYT-066Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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Description
BD-4 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 41 amino acids and having a molecular mass of 4.4kDa.The BD-4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BD-4 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 5-50µg/ml.More Info
-
Introduction
Defensins are cationic peptides with a large spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The Alpha defensins are differentiated from the Beta-defensins by the pairing of their 3 disulfide bonds.
4 human Beta-defensins have been identified to date; BD-1, BD-2, BD-3 and BD-4.
Beta-defensins are expressed on some leukocytes and at epithelial surfaces.
In addition to their direct antimicrobial activities, they are chemoattractant towards immature dendritic cells and memory T cells. The beta-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and, in the case of BD-1 (36 a.a.), a propeptide region. Beta-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Beta-Defensins are 3-5 kDa peptides ranging in size from 33-47 amino acid residues. -
Synonyms
Beta-defensin 4, BD-4, BD-2, Defensin, beta 4, RBD-2, RBD-4, Defb4, Defb2, Defb3.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized BD-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-4 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized BD-4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
QSINNPITCL TKGGVCWGPC TGGFRQIGTC GLPRVRCCKK K.
-
Background
What is the molecular weight/Mw of BD4 Protein?
BD4 Protein has a total Mw of 4.4kDa.
What is the source or expression system of BD4 Protein?
Escherichia Coli.
What is the Purity of BD4 Protein?
BD4 Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of BD4 Protein?
Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 5-50µg/ml.
What is the amino acid sequence of BD4 Protein?
QSINNPITCL TKGGVCWGPC TGGFRQIGTC GLPRVRCCKK K.
What applications can BD4 Protein be used in?
BD4 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BD4 Protein?
The endotoxin level is minimal, BD4 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 :
RARRES2 Human, HisDescription:
Retinoic Acid Receptor Responder 2 Human Recombinant, His Tag
Chemerin, TIG2, Tazarotene-induced gene 2 protein, Retinoic acid receptor responder protein 2, RAR-responsive protein TIG2, RARRES2, HP10433.
Product # :
PRO-1458Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
RARRES2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 158 amino acids (21-157a.a) and having a total molecular mass of 18 kDa. RARRES2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RARRES2 protein solution (1mg/ml) containing 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
-
Introduction
RARRES2 is a secreted chemotactic protein that initiates chemotaxis through the ChemR23 G protein-coupled seven-transmembrane domain ligand. RARRES2 is upregulated by the synthetic retinoid tazarotene and found in a vast variety of tissues. RARRES2 acts as an adipokine, and is truncated on both termini from the proprotein. RARRES2 is structurally related to the cathelicidin precursors, cystatin C and kininogens. RARRES2 promotes calcium mobilization and chemotaxis of immature dendritic cells and macrophages. RARRES2 is secreted as a precursor of little biological activity, which requires proteolytic cleavage of its COOH-terminal domain to be exchangeed into a potent and highly specific agonist of ChemR23. RARRES2 signals via its receptor, ChemR23 (CMKLR1), as a positive regulator of adipocyte differentiation and metabolic function. The Chemerin receptor acts as a coreceptor for SIV and some primary HIV-1 strains. The Chemerin receptor has another ligand, called tazarotene-induced gene.
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Synonyms
Chemerin, TIG2, Tazarotene-induced gene 2 protein, Retinoic acid receptor responder protein 2, RAR-responsive protein TIG2, RARRES2, HP10433.
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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
MGSSHHHHHH SSGLVPRGSH MELTEAQRRG LQVALEEFHK HPPVQWAFQE TSVESAVDTP FPAGIFVRLE FKLQQTSCRK RDWKKPECKV RPNGRKRKCL ACIKLGSEDK VLGRLVHCPI ETQVLREAEE HQETQCLRVQ RAGEDPHSFY FPGQFAFS.
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 :
CRP RatDescription:
C-Reactive Protein Rat Recombinant
Ptx1, C-reactive protein, Pentraxin 1, C-Reactive Protein Pentraxin-Related.
Product # :
PRO-1421Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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- More Info
Description
CRP produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 217 amino acids (20-230 a.a.) and having a molecular mass of 24.1kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40 kDa).CRP is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
CRP 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
-
Introduction
CRP is an acute phase protein that correlates with inflammatory disease and is synthesized by hepatocytes during the acute phase response by certain cytokines (IL-1 and TNF Alpha and Beta). CRP levels increase dramatically (up to 1,000 fold) and serve as a useful marker of inflammation in such conditions as bacterial infection, rheumatoid arthritis, viral infections, transplantation rejection, meningitis, myocardial infarction, septicemia, osteomyelitis and others. CRP is also highly correlated to Serum Amyloid A levels.
-
Synonyms
Ptx1, C-reactive protein, Pentraxin 1, C-Reactive Protein Pentraxin-Related.
-
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
HEDMSKQAFV FPGVSATAYV SLEAESKKPL EAFTVCLYAH ADVSRSFSIF SYATKTSFNE ILLFWTRGQG FSIAVGGPEI LFSASEIPEV PTHICATWES ATGIVELWLD GKPRVRKSLQ KGYIVGTNAS IILGQEQDSY GGGFDANQSL VGDIGDVNMW DFVLSPEQIN AVYVGRVFSP NVLNWRALKY ETHGDVFIKP QLWPLTDCCE SHHHHHH.
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 :
Adiponectin Mouse, HisDescription:
Adiponectin Mouse Recombinant, His Tag
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-537Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- More Info
- sds-page
Description
The Adiponectin Mouse is created as a recombinant protein with a 21 a.a N-terminal fusion of His Tag. The Adiponectin His-Tagged Fusion Protein, produced in E. coli, is a 27.2kDa protein containing 251 amino acid residues of the Acrp30 Mouse, 18-247 amino acids.
Source
Escherichia Coli.
Formulation
Acrp30 Mouse is a sterile filtered liquid formulation containing (1mg/ml) 20mM Tris-HCl pH-8, 1mM DTT and 10% Glycerol.
Purity
Acrp30 Mouse purity is greater than 90% as determined by SDS-PAGE.
sds-page
More Info
-
Introduction
Adiponectin is an adipocyte specific secreted protein that circulates in the plasma. It is induced during adipocyte differentiation and its secretion is stimulated by insulin. Mouse adiponectin shares about 83% amino acid identity with that human. Adiponectin plays a role in various physiological processes such as energy homeostasis and obesity. Adiponectin is reduced in obese humans, and decreased level is associated with insulin resistance and hyperinsulinemia.
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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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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 MEDDVTTTEE LAPALVPPPK GTCAGWMAGI PGHPGHNGTP GRDGRDGTPG EKGEKGDAGL LGPKGETGDV GMTGAEGPRG FPGTPGRKGE PGEAAYVYRS AFSVGLETRV TVPNVPIRFT KIFYNQQNHY DGSTGKFYCN IPGLYYFSYH ITVYMKDVKV SLFKKDKAVL FTYDQYQEKN VDQASGSVLL HLEVGDQVWL QVYGDGDHNG LYADNVNDST FTGFLLYHDT N.
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Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 27.2kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What is the amino acid sequence of ADIPONECTIN Protein?
MGSSHHHHHH SSGLVPRGSH MEDDVTTTEE LAPALVPPPK GTCAGWMAGI PGHPGHNGTP GRDGRDGTPG EKGEKGDAGL LGPKGETGDV GMTGAEGPRG FPGTPGRKGE PGEAAYVYRS AFSVGLETRV TVPNVPIRFT KIFYNQQNHY DGSTGKFYCN IPGLYYFSYH ITVYMKDVKV SLFKKDKAVL FTYDQYQEKN VDQASGSVLL HLEVGDQVWL QVYGDGDHNG LYADNVNDST FTGFLLYHDT N.
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GM- CSF Human, Sf9Description:
Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant, Sf9
CSF-2, MGI-1GM, GMCSF, Pluripoietin-alpha, Molgramostin, Sargramostim.
Product # :
CYT-416Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
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- biological activity
- More Info
Description
GM-CSF Human Recombinant produced in insect cells is a single, glycosylated, polypeptide chain containing 127 amino acids (18-144) and having a molecular mass of 14.6kDa. GM-CSF is fused to a C-terminal His -tag (6x His) and purified by proprietary chromatographic techniques.
Source
Insect Cells.
Formulation
The protein was lyophilized with PBS.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.More Info
-
Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes. -
Synonyms
CSF-2, MGI-1GM, GMCSF, Pluripoietin-alpha, Molgramostin, Sargramostim.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF 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 Granulocyte Macrophage Colony Stimulating Factor 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-Ala-Arg-Ser.
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Background
Recombinant Granulocyte-Macrophage Colony-Stimulating Factor (GMCSF) is a protein that plays a crucial role in the production and differentiation of white blood cells, including granulocytes and macrophages. It is a potent stimulator of hematopoietic stem cells, which are responsible for the production of all blood cells in the body. Recombinant GMCSF is a synthetic version of the protein that is produced using recombinant DNA technology.
Recombinant GMCSF has been extensively studied for its potential therapeutic applications in a variety of medical conditions, including cancer, autoimmune diseases, and infectious diseases. In cancer, GMCSF is used as an immunostimulatory agent to enhance the immune response against cancer cells. By stimulating the production and differentiation of white blood cells, GM-CSF can increase the number of immune cells that can recognize and attack cancer cells. This approach has been successfully used in the treatment of several types of cancer, including melanoma and leukemia.
In autoimmune diseases, recombinant GMCSF has been investigated as a potential treatment for conditions such as rheumatoid arthritis and multiple sclerosis. These diseases are characterized by an overactive immune response that attacks healthy tissues in the body. By modulating the immune response, GMCSF may be able to reduce inflammation and prevent further damage to affected tissues.
In infectious diseases, recombinant GMCSF has been studied as a potential treatment for conditions such as sepsis and HIV/AIDS. In sepsis, a severe bacterial infection, GMCSF may be able to stimulate the production of white blood cells and improve the immune response against the infection. In HIV/AIDS, GMCSF may be able to enhance the immune response against the virus and reduce the risk of opportunistic infections.
Recombinant GMCSF is typically administered by injection, either directly into the affected tissue or into the bloodstream. It is generally well-tolerated, although some patients may experience side effects such as fever, fatigue, and muscle pain.
In conclusion, recombinant GMCSF is a promising therapeutic agent with potential applications in a variety of medical conditions. Its ability to stimulate the production and differentiation of white blood cells makes it a valuable tool in the treatment of cancer, autoimmune diseases, and infectious diseases. Ongoing research is likely to uncover new uses for this protein and further refine its therapeutic potential.
What is the molecular weight/Mw of GM- CSF HUMAN, SF9 Protein?
GM- CSF HUMAN, SF9 Protein has a total Mw of 14.6kDa.
What is the source or expression system of GM- CSF HUMAN, SF9 Protein?
Insect Cells.
What is the Purity of GM- CSF HUMAN, SF9 Protein?
GM- CSF HUMAN, SF9 Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of GM- CSF HUMAN, SF9 Protein?
The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.
What is the amino acid sequence of GM- CSF HUMAN, SF9 Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.
What applications can GM- CSF HUMAN, SF9 Protein be used in?
GM- CSF HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GM- CSF HUMAN, SF9 Protein?
The endotoxin level is minimal, GM- CSF HUMAN, SF9 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 :
GM CSF AntibodyDescription:
Granulocyte Macrophage Colony Stimulating Factor, Mouse Anti-Human
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.
Product # :
ANT-129Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes. -
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.
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Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
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Immunogen
r.Human GM-CSF.
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Ig Subclass
Mouse IgG.
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Clone
NYRhGMCSF.
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Applications
Direct ELISA, Western Blot, Immuneprecipitation.
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Titer
By direct ELISA, 1:10,000 dilution will yield 0.4 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
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Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
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Purification Method
Ion exchange Protein concentration1mg/ml in PBS (after reconstitution).
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 :
Enterokinase BovineDescription:
Enteropeptidase/ Enterokinase Light Chain Bovine Recombinant
Enteropeptidase, EC 3.4.21.9, Enterokinase, Serine protease 7, ENTK, MGC133046.
Product # :
ENZ-311Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Enterokinase (rEK) Bovine Recombinant is the catalytic subunit of bovine enterokinase, which is expressed by E. Coli and purified to yield a high enzyme activity preparation. EK recognizes the sequence Asp-Asp-Asp-Asp-Lys and cleaves the peptide bond after the lysine residue. The enzyme can be used to cleave any fusion protein that carries this sequence. Recombinant Bovine Enterokinase is a single glycosylated polypeptide chain containing 235 amino acids and having an MW of ~28kDa.
Source
E. Coli.
Formulation
Bovine EK in 50mM Tris-HCl, pH 8.0, 0.5M NaCl and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Enteropeptidase or enterokinase is an enzyme involved in human digestion. It is produced by cells in the duodenum wall, and is secreted from duodenum's glands, the crypts of Lieberk?hn, whenever ingested food enters the duodenum from the stomach. Enteropeptidase has the critical job of turning trypsinogen (a zymogen) to trypsin, indirectly activating a number of pancreatic digestive enzymes. Enteropeptidase is a serine protease enzyme (EC 3.4.21.9). Enteropeptidase is a part of the Chymotrypsin-clan of serine proteases, and is structurally similar to these proteins.
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Synonyms
Enteropeptidase, EC 3.4.21.9, Enterokinase, Serine protease 7, ENTK, MGC133046.
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Physical Appearance
Sterile liquid solution.
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Stability
One year when stored at –20°C. Please avoid freeze-thaw cycles.
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Unit Definition
One unit is defined as the amount of enzyme needed to cleave 50µg of fusion protein in 16 hours to 95% completion at 25°C in a buffer containing 25mM Tris-HCl, pH 7.6, 50mM NaCl, and 2mM CaCl2.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
HSA, Pichia PastorisDescription:
Human Serum Albumin Recombinant, Pichia
Serum albumin, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.
Product # :
PRO-2149Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HSA Human Recombinant produced in Pichia Pastoris is a polypeptide chain containing 585 amino acids and having a molecular mass of 67 kDa.The recombinant Albumin is purified by proprietary chromatographic techniques.
Source
Pichia Pastoris.
Formulation
The Recombinant Albumin having a concentration of 200mg/ml contains 140mM sodium chloride and 0.16mM octanoate.
Purity
Greater than 97% as determined by HPLC.
More Info
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Introduction
Albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin. Albumin is a soluble, monomeric protein which comprises about one-half of the blood serum protein. Albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. Albumin is a globular unglycosylated serum protein of molecular weight 65,000. The human albumin gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
HSA is widely used to stabilize blood volume generally from donors but the fear of contamination such as HIV & Hepatitis has enticed great interest in the recombinant form which is identical to the natural blood. -
Synonyms
Serum albumin, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.
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Physical Appearance
Yellowish gel like solution.
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Stability
Recombinant Albumin although stable at 15°C for 1 week, should be stored at 4°C for longer periods of time.Please prevent freeze-thaw cycles.
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Applications
Recombinant Albumin can be used as a media culture supplement at concentrations up to 5 grams per liter. Gradual adaptation of cell lines over several passages to a concentration of 0.5gr to 2gr per liter.
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 :
PramlintideDescription:
Pramlintide
Product # :
HOR-300Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Pramlintide Synthetic is a single, non-glycosylated polypeptide chain containing 37 amino acids, having a molecular mass of 3949.4 Dalton and a Molecular formula of C171H267N51O53S2.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Pramlintide acetate is a hormone that is released into the bloodstream, in a similar pattern as insulin. Pramlintide aids in the absorption of glucose by slowing gastric emptying, promoting satiety, and inhibiting inappropriate secretion of glucagon, a catabolic hormone that opposes the effects of insulin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Pramlintide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Pramlintide 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 Pramlintide in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions. The Pramlintide is also soluble in 1% Acetic Acid.
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Amino Acid Sequence
KCNTATCATNRLANFLVHSSNNFGPILPPTNVGSNTY-NH2.
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 :
CCL20 MouseDescription:
Macrophage Inflammatory Protein-3 alpha Mouse Recombinant (CCL20)
Small inducible cytokine A20 precursor, CCL20, Macrophage inflammatory protein 3 alpha, MIP-3-alpha, Liver and activation- regulated chemokine, CC chemokine LARC, Beta chemokine exodus-1, CKb4, LARC, ST38, MIP3A, MIP-3a, SCYA20, C-C motif chemokine 20, CC chemokine ST38, exodus-1.
Product # :
CHM-236Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- source
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- purity
- biological activity
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Description
Macrophage Inflammatory Protein-3 alpha Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.9 kDa. The MIP-3a is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Activity is calculated by its ability to chemoattract primary human T cells at 2-20ng/ml, corresponding to a specific activity of 50,000-500,000 units/mg.
More Info
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Introduction
CCL20 is a chemotactic factor that draws lymphocytes & neutrophils, rather than monocytes. MIP-3 alpha inhibits proliferation of myeloid progenitors in colony formation assays. MIP3A plays a role in the formation and function of the mucosal lymphoid tissues by attracting lymphocytes and dendritic cells towards epithelial cells. C-terminal processed forms have been shown to be equally chemotactically active for leukocytes. CCL20 holdes antibacterial activity e.coli atcc 25922 and s.aureus atcc 29213. CCL20 gene transcription is activated by H. pylori, which activates NF-kappaB through intracellular signal pathway which involves IkappaB kinase and NF-kappaB-inducing kinase. MIP-3 alpha is invloved in chemokine-mediated lymphocyte trafficking during gastric inflammation in Helicobacter infection. CCL20 expression is involved in the recruitment of CD45R0-positive T cell subsets into the intestinal lamina propria.
MIP-3A is in charge of the advancement of pulpal inflammation through the recruitment of C-C motif Receptor 6-expressing lymphocytes Vaginal epithelial cells respond to factors present in semen by secreting MIP-3 alpha, which increases langerhans cells recruitment during HIV transmission. -
Synonyms
Small inducible cytokine A20 precursor, CCL20, Macrophage inflammatory protein 3 alpha, MIP-3-alpha, Liver and activation- regulated chemokine, CC chemokine LARC, Beta chemokine exodus-1, CKb4, LARC, ST38, MIP3A, MIP-3a, SCYA20, C-C motif chemokine 20, CC chemokine ST38, exodus-1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIP-3a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL-20 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 MIP-3a 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
ASNYDCCLSY IQTPLPSRAI VGFTRQMADE ACDINAIIFH TKKRKSVCAD PKQNWVKRAV NLLSLRVKKM.
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Background
What is the molecular weight/Mw of CCL20 MOUSE Protein?
CCL20 MOUSE Protein has a total Mw of 7.9kDa.
What is the source or expression system of CCL20 MOUSE Protein?
Escherichia Coli.
What is the Purity of CCL20 MOUSE Protein?
CCL20 MOUSE Protein is > 95% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL20 MOUSE Protein?
The Activity is calculated by its ability to chemoattract primary human T cells at 2-20ng/ml, corresponding to a specific activity of 50,000-500,000 units/mg.
What is the amino acid sequence of CCL20 MOUSE Protein?
ASNYDCCLSY IQTPLPSRAI VGFTRQMADE ACDINAIIFH TKKRKSVCAD PKQNWVKRAV NLLSLRVKKM.
What applications can CCL20 MOUSE Protein be used in?
CCL20 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL20 MOUSE Protein?
The endotoxin level is minimal, CCL20 MOUSE 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 :
BD 1 HumanDescription:
Beta Defensin-1 Human Recombinant
Beta-defensin 1, BD-1, Defensin beta 1, hBD-1, HBD1, HBP1, DEFB1, HBD-1, HBP-1, DEFB101, DEFB-1, MGC51822.
Product # :
CYT-564Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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Description
Beta Defensin-1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 47 amino acids and having a molecular mass of 5 kDa.The BD-1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Human BD-1 was lyophilized from a concentrated (1mg/ml) solution containing 20mM PBS pH-7.4 and 130mM sodium chloride.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract CD34+ dendritic cells using a concentration range of 100-1000ng/ml corresponding to a specific activity of 1,000-10,000IU/mg.More Info
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Synonyms
Beta-defensin 1, BD-1, Defensin beta 1, hBD-1, HBD1, HBP1, DEFB1, HBD-1, HBP-1, DEFB101, DEFB-1, MGC51822.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Beta Defensin-1 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-1 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 Beta Defensin-1 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
GNFLTGLGHR SDHYNCVSSG GQCLYSACPI FTKIQGTCYR GKAKCCK.
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Background
Beta Defensin-1 Human Recombinant: Unveiling its Potential in Innate Immunity and Therapeutic Applications
Abstract:
Beta Defensin-1 (BD-1), a member of the defensin family, plays a crucial role in innate immunity and host defense. This research paper provides an overview of BD-1 human recombinant, exploring its molecular characteristics, antimicrobial properties, and therapeutic applications. Understanding the multifaceted role of BD-1 offers new avenues for developing innovative immunotherapies. This article offers a concise analysis of BD-1, highlighting its impact on innate immunity and its therapeutic potential.Introduction:
Innate immunity serves as the first line of defense against invading pathogens. BD-1, a key peptide within the defensin family, exhibits broad-spectrum antimicrobial activity and plays a pivotal role in host defense mechanisms. This paper provides an overview of BD-1, shedding light on its structure, function, and therapeutic potential.BD-1 Structure and Function:
BD-1 is a cationic peptide with a conserved cysteine motif that confers its antimicrobial properties. It acts by disrupting the integrity of microbial cell membranes, leading to microbial death. Additionally, BD-1 exhibits immunomodulatory effects by stimulating immune cell recruitment and cytokine production.Antimicrobial Properties and Therapeutic Applications:
BD-1 demonstrates antimicrobial activity against a wide range of pathogens, including bacteria, fungi, and viruses. Its ability to combat multidrug-resistant strains makes it an attractive candidate for the development of novel antimicrobial therapies. Furthermore, BD-1's immunomodulatory effects contribute to its potential in treating inflammatory and infectious diseases.Therapeutic Potential of BD-1 Human Recombinant:
BD-1 human recombinant holds significant promise in the field of immunotherapy. Strategies aimed at enhancing BD-1 expression or delivering exogenous BD-1 may help boost innate immune responses in patients with compromised immune systems or chronic infections. Furthermore, BD-1-based therapeutics could be developed to combat antibiotic-resistant infections and prevent biofilm formation.Challenges and Future Directions:
While BD-1 shows immense therapeutic potential, challenges must be addressed. Further research is necessary to optimize the delivery methods of BD-1 and evaluate its long-term safety and efficacy. Additionally, understanding the interplay between BD-1 and other immune factors will aid in developing combinatorial approaches for enhanced therapeutic outcomes.Conclusion:
BD-1 human recombinant represents a promising avenue for developing novel immunotherapies and combating antimicrobial resistance. Understanding the molecular mechanisms and functional implications of BD-1 in innate immunity opens new horizons for innovative treatments. Continued research in this field has the potential to revolutionize the field of immunotherapy and improve patient outcomes.What is the molecular weight/Mw of BD1 Protein?
BD1 Protein has a total Mw of 5kDa.
What is the source or expression system of BD1 Protein?
Escherichia Coli.
What is the Purity of BD1 Protein?
BD1 Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of BD1 Protein?
Determined by its ability to chemoattract CD34+ dendritic cells using a concentration range of 100-1000ng/ml corresponding to a specific activity of 1,000-10,000IU/mg.
What is the amino acid sequence of BD1 Protein?
GNFLTGLGHR SDHYNCVSSG GQCLYSACPI FTKIQGTCYR GKAKCCK.
What applications can BD1 Protein be used in?
BD1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BD1 Protein?
The endotoxin level is minimal, BD1 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.