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1000 results found for “dysbindin”
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Name :
PDZK1 AntibodyDescription:
PDZ Domain Containing 1, Mouse Anti Human
PDZ Domain Containing 1, PDZ-Containing Kidney Protein 1, Na(+)/H(+) Exchange Regulatory Cofactor NHE-RF3, Na/Pi Cotransporter C-Terminal-Associated Protein 1, Sodium-Hydrogen Exchanger Regulatory Factor 3, CFTR-Associated Protein Of 70 KDa, NHERF-3, CAP70, PDZD1, CLAMP, naPi-Cap1.
Product # :
ANT-460Price :
Quantity :
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Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
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Introduction
PDZK1 is a PDZ domain-containing scaffolding protein which facilitates localization of cell surface proteins and has a key part in cholesterol metabolism by regulating the HDL receptor, scavenger receptor class B type 1. Single nucleotide polymorphism in this gene is linked to metabolic syndrome, and overexpression results in drug resistance of multiple myeloma.
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Synonyms
PDZ Domain Containing 1, PDZ-Containing Kidney Protein 1, Na(+)/H(+) Exchange Regulatory Cofactor NHE-RF3, Na/Pi Cotransporter C-Terminal-Associated Protein 1, Sodium-Hydrogen Exchanger Regulatory Factor 3, CFTR-Associated Protein Of 70 KDa, NHERF-3, CAP70, PDZD1, CLAMP, naPi-Cap1.
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Physical Appearance
Sterile Filtered colorless solution.
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Immunogen
Anti-human PDZK1 mAb, clone PAT1A2A, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human PDZK1 protein 1-519 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chain and Kappa light chain.
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Clone
PAT1A2AT.
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Applications
The 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 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
PDZK1 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 :
NT 3 HumanDescription:
Neurotrophin-3 Human Recombinant
Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.
Product # :
CYT-257Price :
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Shipped at Room temp
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Description
Neurotrophin-3 Human Recombinant produced in E.Coli is a non-glycosylated and non-covalently linked homodimer, containing 2x120 amino acid chains, having a total Mw of 27.5 kDa. The NT-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from 0.1% TFA.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Biological Activity
The ED50 as determined by the dose-dependent proliferation of neuroblastoma cell line expressing BR6 is 3.49 ng/ml.
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Introduction
NT3 a member of the neurotrophin family, that controls survival and differentiation of mammalian neurons. This protein is closely related to both nerve growth factor and brain-derived neurotrophic factor. It may be involved in the maintenance of the adult nervous system, and may affect development of neurons in the embryo when it is expressed in human placenta. NTF3-deficient mice generated by gene targeting display severe movement defects of the limbs. The mature peptide of this protein is identical in all mammals examined including human, pig, rat and mouse.
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Synonyms
Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized NGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NGF-2 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 Neurotrophin-3 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
MYAEHKSHRGE YSVCDSESLW VTDKSSAIDI RGHQVTVLGE IKTGNSPVKQ YFYETRCKEA RPVKNGCRGI DDKHWNSQCK TSQTYVRALT SENNKLVGWR WIRIDTSCVC ALSRKIGRT.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 2.165 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of NT-3 as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Borrelia DbpBDescription:
Borrelia Burgdorferi Decorin Binding Protein B Recombinant
Product # :
BOR-007Price :
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Shipped with Ice Packs
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Description
Recombinant Borrelia Burgdorferi Decorin Binding Protein B produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 19,353 Dalton. Borrelia DbpB is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Borrelia DbpB (1.11mg/1ml) is supplied in 16mM HEPES buffer pH-8.0, 300mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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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.
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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.
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Applications
Western blot with Lyme positive 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.
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Name :
Inhibin alpha A Chain HumanDescription:
Inhibin-Alpha A Chain Human Recombinant
Inhibin-Alpha, A-Inhibin Subunit, Inhibin Alpha Chain, INHA.
Product # :
HOR-293Price :
Quantity :
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Shipped with Ice Packs
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Description
Inhibin-Alpha A chain Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids fragment (233-366) and having an amino-terminal hexahistidine tag, having a total molecular weight of 19.2 kDa. The Inhibin-Alpha A chain is purified by standard chromatographic techniques.
Source
Escherichia Coli.
Formulation
Inhibin-A alpha chain is supplied in 20mM Tris HCl (pH-8), 5mM EDTA and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development. -
Synonyms
Inhibin-Alpha, A-Inhibin Subunit, Inhibin Alpha Chain, INHA.
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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. Please avoid freeze thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DCN MouseDescription:
Decorin Mouse Recombinant
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN.
Product # :
PRO-2234Price :
Quantity :
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Shipped with Ice Packs
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Description
DCN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (17-354 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 344 amino acids and having a molecular mass of 38.8kDa.DCN shows multiple bands between 40-57kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
DCN protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 30% glycerol and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.
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Synonyms
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN.
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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
GPFEQRGLFD FMLEDEASGI IPYDPDNPLI SMCPYRCQCH LRVVQCSDLG LDKVPWDFPP DTTLLDLQNN KITEIKEGAF KNLKDLHTLI LVNNKISKIS PEAFKPLVKL ERLYLSKNQL KELPEKMPRT LQELRVHENE ITKLRKSDFN GLNNVLVIEL GGNPLKNSGI ENGAFQGLKS LSYIRISDTN ITAIPQGLPT SLTEVHLDGN KITKVDAPSL KGLINLSKLG LSFNSITVME NGSLANVPHL RELHLDNNKL LRVPAGLAQH KYIQVVYLHN NNISAVGQND FCRAGHPSRK ASYSAVSLYG NPVRYWEIFP NTFRCVYVRS AIQLGNYKHH HHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DLST HumanDescription:
Dihydrolipoamide S-Succinyltransferase Human Recombinant
dihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex), Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex, component E2, DLST, E2K, OGDC-E2, EC 2.3.1.61, EC 2.3.1.
Product # :
ENZ-083Price :
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Shipped with Ice Packs
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Description
DLST is a Full-length cDNA coding for the mature form of the human OGDC-E2 protein having a molecular mass of 42,301 Dalton (pH 6.3).DLST protein is fused to a hexa-histidine purification tag.
Source
Sf9 insect cells.
Formulation
DLST (0.74mg/ml) is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.
Purity
DLST purity was found to be greater than 75% as determined by SDS-PAGE.
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Introduction
DLST catalyzes the general transformation of 2-oxoglutarate to succinyl-CoA and CO(2). DLST holds multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
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Synonyms
dihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex), Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex, component E2, DLST, E2K, OGDC-E2, EC 2.3.1.61, EC 2.3.1.
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Stability
Store DLST 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. DLST binds IgG-type human auto-antibodies. 2. Standard ELISA test (checkerboard analysis of positive/negative sera panels); immunodot test with positive/negative sera panels.
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coating concentration
0.4-1.0 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for biotinylation and iodination.
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Applications
Western blot with anti-M2-Antigen autoantibody-positive patient sera or monoclonal
anti-hexa-His-tag antibody.
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 :
CABP7 HumanDescription:
Calcium Binding Protein 7 Human Recombinant
Calcium-binding protein 7, CaBP7, Calneuron II, Calneuron-2, CABP7, CALN2.
Product # :
PRO-211Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CABP7 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 208 amino acids (1-188 a.a.) and having a molecular mass of 23.7kDa.CABP7 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CABP7 protein solution (0.5mg/ml) containing Phosphate-buffered saline (pH 7.4).
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Calcium-binding protein 7 (CABP7) contains 2 EF-hand domains. CABP7 negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. The CaBP family of EF-hand containing small Ca (2+)-binding proteins has lately emerged as significant regulators of multiple targets essential to normal neuronal function in the mammalian central nervous system.
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Synonyms
Calcium-binding protein 7, CaBP7, Calneuron II, Calneuron-2, CABP7, CALN2.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
CABP7 Human Recombinant 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
MGSSHHHHHH SSGLVPRGSH MPFHPVTAAL MYRGIYTVPN LLSEQRPVDI PEDELEEIRE AFKVFDRDGN GFISKQELGT AMRSLGYMPN EVELEVIIQR LDMDGDGQVD FEEFVTLLGP KLSTSGIPEK FHGTDFDTVF WKCDMQKLTV DELKRLLYDT FCEHLSMKDI ENIIMTEEES HLGTAEECPV DVETCSNQQI RQTCVRKS.
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 :
Resistin Human (64-110)Description:
Resistin (64-110) Human Recombinant
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF.
Product # :
CYT-1232Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Resistin Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The Resistin His-Tagged Fusion Protein, produced in E. coli, is a 12kDa protein containing 47 amino acid residues of the Resistin Human, 64-110 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Synonyms
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized Resistin at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Background
Human resistin is an adipokine primarily secreted by adipose tissue, mainly in response to obesity and inflammatory conditions.
Resistin Function
Resistin takes part in insulin resistance, which can be the cause of the development of type 2 diabetes. Resistin can also affect glucose metabolism and insulin signalling.
Regulation
Levels of resistin are influenced by factors such as inflammation, obesity and certain hormones. It tends to increase in conditions associated with obesity and metabolic syndrome.
Clinical Relevance
Elevated levels of resistin have been associated with obesity-related conditions, cardiovascular diseases, and metabolic disorders. Resisting is considered as a potential biomarker for these conditions.
Resistin Mechanism
Resistin promotes insulin resistance through different pathways such as the modulation of inflammatory processes and the inhibition of insulin signaling in target tissues like liver and muscle.
Research
Ongoing studies are exploring resistin’s role in metabolic regulation, the exact mechanisms of action of resistin and its potential as a therapeutic target for treating metabolic diseases.
Overall, resistin is a critical factor in metabolic health, mainly in the context of diabetes and obesity.
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 :
S100A8 MouseDescription:
S100 Calcium Binding Protein A8 Mouse Recombinant
Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.
Product # :
PRO-233Price :
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Shipped with Ice Packs
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Description
S100A8 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids (1-89a.a) and having a molecular mass of 12.4kDa.S100A8 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
S100A8 protein solution (1mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.
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Synonyms
Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPSELEKALS NLIDVYHNYS NIQGNHHALY KNDFKKMVTT ECPQFVQNIN IENLFRELDI NSDNAINFEE FLAMVIKVGV ASHKDSHKE
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 :
CAMLG HumanDescription:
Calcium Modulating Ligand Human Recombinant
Calcium Modulating Ligand, Calcium-Modulating Cyclophilin Ligand, Calcium-Signal Modulating Cyclophilin Ligand, Cyclophilin B-Binding Protein, CAML.
Product # :
PRO-1612Price :
Quantity :
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Shipped with Ice Packs
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Description
CAMLG Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-189) and having a molecular mass of 23.2kDa.CAMLG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CAMLG solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
CAMLG binds to cyclophilin B and operates downstream of the TCR and upstream of calcineurin by causing an influx of calcium. CAMLG is an essential membrane protein that takes part in the calcium signal transduction pathway, connecting cyclophilin B to calcium signaling.
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Synonyms
Calcium Modulating Ligand, Calcium-Modulating Cyclophilin Ligand, Calcium-Signal Modulating Cyclophilin Ligand, Cyclophilin B-Binding Protein, CAML.
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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 MGSMESMAVA TDGGERPGVP AGSGLSASQR RAELRRRKLL MNSEQRINRI MGFHRPGSGA EEESQTKSKQ QDSDKLNSLS VPSVSKRVVL GDSVSTGTTD QQGGVAEVKG TQLGDKLDSF IKPPECSSDV NLELRQRNRG DLTADSVQRG SRHGLEQYLS RFEEAMKLRK QLISEKPSQE DGNTTEEFDS FR
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 :
BD 3 HumanDescription:
Beta Defensin-3 Human Recombinant
HBD3, HBP3, DEFB3, HBD-3, HBP-3, DEFB103.
Product # :
CYT-461Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Beta Defensin-3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 45 amino acids and having a molecular mass of 5161.2 Dalton. The BD-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HBD-3 was lyophilized without additives.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 103A, which has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense.
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Synonyms
HBD3, HBP3, DEFB3, HBD-3, HBP-3, DEFB103.
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Physical Appearance
Sterile Filtered lyophilized (freeze-dried) powder.
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Stability
Lyophilized Beta Defensin-3 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-3 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-3 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
GIINTLQKYY CRVRGGRCAV LSCLPKEEQI GKCSTRGRKC CRRKK.
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Background
Beta Defensin-3 Human Recombinant: Advancements in Antimicrobial Peptide Therapy
Abstract:
Beta Defensin-3 (hBD-3) human recombinant is a promising antimicrobial peptide with broad-spectrum activity against bacteria, viruses, and fungi. This research paper provides an overview of hBD-3, including its properties, mode of action, and potential applications. Additionally, novel methodologies for the production and optimization of hBD-3 human recombinant are discussed, highlighting its future implications in the field of infectious disease management.Introduction:
The rise of drug-resistant pathogens necessitates exploring alternative therapeutic approaches, such as antimicrobial peptides. Beta Defensin-3 (hBD-3) human recombinant has emerged as a potent candidate due to its broad-spectrum antimicrobial activity. This paper aims to examine the unique features of hBD-3 and propose innovative methodologies for its production and optimization.Properties and Mode of Action:
hBD-3 possesses a distinct structural composition consisting of 45 amino acids, including an N-terminal loop, three antiparallel β-strands, and a C-terminal α-helix. These structural elements contribute to its ability to disrupt microbial membranes and target selectivity. The mode of action involves electrostatic interactions with negatively charged microbial membranes, leading to membrane disruption and subsequent cell death. Furthermore, hBD-3 exhibits immunomodulatory functions by promoting chemotaxis, enhancing phagocytic activity, and modulating the release of pro-inflammatory cytokines.Production of hBD-3 Human Recombinant:
Various expression systems, such as bacterial, yeast, and mammalian cell-based platforms, have been explored for the efficient production of hBD-3 human recombinant. Each system offers distinct advantages and challenges, requiring careful selection to achieve high yields and desired protein quality. Optimization strategies, including codon optimization, fusion protein tags, and appropriate growth conditions, have been employed to enhance production efficiency. Purification techniques, such as chromatography and ultrafiltration, have been optimized to isolate high-quality hBD-3 recombinant.Applications and Future Perspectives:
hBD-3 human recombinant exhibits significant therapeutic potential against drug-resistant pathogens, making it a promising alternative to conventional antibiotics. It also demonstrates promise in wound healing and tissue regeneration by stimulating angiogenesis, extracellular matrix production, and keratinocyte migration. Moreover, the unique physicochemical properties of hBD-3 open avenues for its utilization in nanomedicine, enabling targeted therapy and improved drug delivery.Conclusion:
hBD-3 human recombinant represents a potent antimicrobial peptide with broad-spectrum activity against diverse pathogens. The optimization of production methodologies and further exploration of its mechanisms of action will contribute to its clinical utility. With its potential applications in infectious disease management, wound healing, and nanomedicine, hBD-3 human recombinant holds promise as a versatile therapeutic agent.What is the molecular weight/Mw of BD3 Protein?
BD3 Protein has a total Mw of 5.1kDa.
What is the source or expression system of BD3 Protein?
Escherichia Coli.
What is the Purity of BD3 Protein?
BD3 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BD3 Protein?
The biological functionality of BD3 Protein will be determined in the future.
What is the amino acid sequence of BD3 Protein?
GIINTLQKYY CRVRGGRCAV LSCLPKEEQI GKCSTRGRKC CRRKK.
What applications can BD3 Protein be used in?
BD3 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BD3 Protein?
The endotoxin level is minimal, BD3 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 :
SARS MERS RBD, ActiveDescription:
SARS MERS Spike Receptor Binding Domain Recombinant, Active
Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERS, MERSCoV RBD, MERS RBD, receptor binding domain, RBD, Spike RBD protein, Spike glycoprotein, S glycoprotein, E2, Peplomer protein
Product # :
SARS-060Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SARS MERS RBD Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 258 amino acids (358-606 aa) and having a molecular mass of 28.2kDa. SARS MERS RBD is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The SARS MERS RBD solution (0.5mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured by its binding ability in a functional ELISA with Human DPPIV/CD26 (CAT# enz-1187).
More Info
-
Synonyms
Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERS, MERSCoV RBD, MERS RBD, receptor binding domain, RBD, Spike RBD protein, Spike glycoprotein, S glycoprotein, E2, Peplomer protein
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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
ADPSGVYSVS SFEAKPSGSV VEQAEGVECD FSPLLSGTPP QVYNFKRLVF TNCNYNLTKL LSLFSVNDFT CSQISPAAIA SNCYSSLILD YFSYPLSMKS DLSVSSAGPI SQFNYKQSFS NPTCLILATV PHNLTTITKP LKYSYINKCS RLLSDDRTEV PQLVNANQYS PCVSIVPSTV WEDGDYYRKQ LSPLEGGGWL VASGSTVAMT EQLQMGFGIT VQYGTDTNSV CPKLEFANDT KIASQLGNCV EYHHHHHH.
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Background
The severe acute respiratory syndrome coronavirus (SARS-CoV) and Middle East respiratory syndrome coronavirus (MERS-CoV) have posed significant global health threats in recent years. Central to their pathogenesis is the interaction between the viral spike proteins and host cell receptors. This research aims to investigate the receptor binding domain (RBD) of SARS and MERS spike proteins and its implications for viral entry and the development of therapeutic interventions. Understanding the molecular mechanisms underlying viral-host interactions can pave the way for targeted therapeutic strategies against these deadly coronaviruses.
Structure and Function of SARS and MERS Spike RBD:
The spike proteins of SARS-CoV and MERS-CoV are critical for viral entry into host cells. These proteins consist of two subunits: S1, responsible for receptor binding, and S2, involved in membrane fusion. The receptor binding domain (RBD) within the S1 subunit specifically interacts with host cell receptors, enabling viral attachment and entry. The RBDs of SARS and MERS spike proteins exhibit unique structural features and binding affinities for their respective receptors.
Interaction with ACE2 and DPP4 Receptors:
The SARS-CoV spike protein RBD interacts with the angiotensin-converting enzyme 2 (ACE2) receptor, which is abundantly expressed in the respiratory tract. The binding of SARS-CoV RBD to ACE2 facilitates viral entry into host cells. On the other hand, the MERS-CoV spike protein RBD interacts with the dipeptidyl peptidase 4 (DPP4) receptor, predominantly expressed in the lungs and other tissues. The ACE2 and DPP4 receptors play crucial roles in determining the host range and tissue tropism of SARS and MERS coronaviruses.
Implications for Viral Pathogenesis:
The binding of SARS and MERS spike RBDs to their respective receptors triggers conformational changes in the spike protein, leading to membrane fusion and subsequent viral entry. This process is crucial for viral replication and the spread of infection within the host. The specificity and affinity of the RBD-receptor interaction influence viral tropism, tissue damage, and disease severity. Understanding the determinants of RBD-receptor binding can provide insights into viral pathogenesis and potential therapeutic targets.
Development of Therapeutic Interventions:
The RBD of SARS and MERS spike proteins represents a promising target for the development of antiviral therapeutics. Several strategies have been explored, including monoclonal antibodies and small molecule inhibitors, to disrupt the RBD-receptor interaction and inhibit viral entry. These approaches aim to block the binding interface between the spike RBD and the host receptor, thereby preventing viral attachment and entry. Additionally, vaccine development efforts have focused on generating neutralizing antibodies against the RBD to elicit protective immune responses.
Conclusion:
The investigation of the receptor binding domain (RBD) of SARS and MERS spike proteins sheds light on the molecular mechanisms underlying viral entry and pathogenesis. The specific interactions between the spike RBD and host cell receptors play a crucial role in determining viral tropism and tissue damage. Targeting the RBD-receptor interaction holds promise for the development of effective therapeutics against SARS-CoV, MERS-CoV, and potentially other related coronaviruses. Further research and development efforts are needed to exploit the potential of the spike RBD as a therapeutic target and to combat future coronavirus outbreaks.
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 :
Myostatin HumanDescription:
Myostatin Human Recombinant
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
Product # :
CYT-418Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
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- biological activity
- More Info
Description
Myostatin Human Recombinant produced in E.Coli is a homodimer, non-glycosylated polypeptide chain containing 2 x 109 amino acids and having a total molecular mass of 24814 Dalton. The GDF-8 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing no additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the inhibition of the proliferation of MPC-11 cells is < 20ng/ml, corresponding to a Specific Activity of 50,000units/mg.More Info
-
Introduction
GDF8 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.
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Synonyms
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Myostatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Myostatin 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 Myostatin in sterile 20mM HCl at 0.1 mg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Asp-Phe-Gly-Leu-Asp.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.55 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of Myostatin as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
DLL4 MouseDescription:
Delta-Like 4 Mouse Recombinant
Delta-like protein 4, Drosophila Delta homolog 4, Delta 4, Dll4.
Product # :
PRO-2236Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
DLL4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (27-532 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 512 amino acids and having a molecular mass of 55.8kDa.DLL4 shows multiple bands between 50-70kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
DLL4 protein solution (1mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Delta-Like4, also known as DLL4 is implicated in the Notch signaling pathway as Notch ligand. Consequently DLL4 negatively regulates endothelial cell proliferation, migration as well as angiogenic sprouting. DLL4 is vital for retinal progenitor proliferation and also required for suppressing rod fates in late retinal progenitors and for proper generation of other retinal cell types. Furthermore, at some stage in the spinal cord neurogenesis, DLL4 inhibits V2a interneuron fate.
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Synonyms
Delta-like protein 4, Drosophila Delta homolog 4, Delta 4, Dll4.
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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
GSGIFQLRLQ EFVNQRGMLA NGQSCEPGCR TFFRICLKHF QATFSEGPCT FGNVSTPVLG TNSFVVRDKN SGSGRNPLQL PFNFTWPGTF SLNIQAWHTP GDDLRPETSP GNSLISQIII QGSLAVGKIW RTDEQNDTLT RLSYSYRVIC SDNYYGESCS RLCKKRDDHF GHYECQPDGS LSCLPGWTGK YCDQPICLSG CHEQNGYCSK PDECICRPGW QGRLCNECIP HNGCRHGTCS IPWQCACDEG WGGLFCDQDL NYCTHHSPCK NGSTCSNSGP KGYTCTCLPG YTGEHCELGL SKCASNPCRN GGSCKDQENS YHCLCPPGYY GQHCEHSTLT CADSPCFNGG SCRERNQGSS YACECPPNFT GSNCEKKVDR CTSNPCANGG QCQNRGPSRT CRCRPGFTGT HCELHISDCA RSPCAHGGTC HDLENGPVCT CPAGFSGRRC EVRITHDACA SGPCFNGATC YTGLSPNNFV CNCPYGFVGS RCEFPVGLPP SFPWVAHHHH HH
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 :
ID1 HumanDescription:
Inhibitor of DNA Binding 1 Human Recombinant
bHLHb24, ID, DNA-binding protein inhibitor ID-1, Class B basic helix-loop-helix protein 24, Inhibitor of DNA binding 1, ID1.
Product # :
PRO-1426Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ID1 Human Recombinant produced in E. coli is a single polypeptide chain containing 178 amino acids (1-155) and having a molecular mass of 18.5kDa. ID1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ID1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Inhibitor of DNA Binding 1 (ID1) is a helix-loop-helix protein which can form heterodimers with members of the basic HLH family of transcription factors. ID1 is lacking DNA binding activity and thus can inhibit the DNA binding and transcriptional activation ability of basic HLH proteins with which it interacts. ID1 participates in cell growth, senescence, and differentiation.
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Synonyms
bHLHb24, ID, DNA-binding protein inhibitor ID-1, Class B basic helix-loop-helix protein 24, Inhibitor of DNA binding 1, ID1.
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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 MGSMKVASGS TATAAAGPSC ALKAGKTASG AGEVVRCLSE QSVAISRCAG GAGARLPALL DEQQVNVLLY DMNGCYSRLK ELVPTLPQNR KVSKVEILQH VIDYIRDLQL ELNSESEVGT PGGRGLPVRA PLSTLNGEIS ALTAEAACVP ADDRILCR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Activin B HumanDescription:
Activin-B Human Recombinant
Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.
Product # :
CYT-058Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Activin B human Recombinant produced in Nicotiana benthamiana plant is a beta-B single chain (aa 293-406) containing 123 amino acids (molecular formula C615H910N178O177S12). Activin B is fused to a 10-His-tag at the N-terminal having the total molecular mass of 14kDa and purified by standard chromatographic techniques.
Source
Nicotiana benthamiana plant
Formulation
Lyophilized from 1mg/ml solution in 0.05M Tris-HCl buffer pH 7.4.
Purity
Greater than 97.0% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development. -
Synonyms
Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Activin B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin B 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 Activin B 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
HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG
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Background
What is the molecular weight / Mw of Activin B Protein?
Activin A Protein has a total Mw of 14 kDa.
What is the source or expression system of Activin B Protein?
Nicotinia
What is the Purity of Activin B Protein?
Activin B Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin B Protein?
The biological functionality of Activin-B Protein will be determined in the future.
What is the endotoxin level for Activin B Protein?
The endotoxin level is minimal, ACTIVIN B Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of ACTIVIN B Protein?
HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG
What applications can ACTIVIN B Protein be used in?
ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
DEFB116 HumanDescription:
Beta Defensin 116 Human Recombinant
Beta-Defensin 16, DEFB-16, Beta 16, defensin, Beta-Defensin 116, Defensin, Beta 16, DEFB16.
Product # :
CYT-713Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
DEFB116 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 102 amino acids (24-102 a.a) and having a molecular mass of 11.5kDa.DEFB116 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DEFB116 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Beta Defensin 116, also known as DEFB116 is a member of the beta-defensin family.DEFB116 has antibacterial activity. The innate immune system includes antimicrobial peptides that protect multicellular organisms from a diverse spectrum of microorganisms. In addition, Beta-Defensins contain one important family of mammalian antimicrobial peptides.
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Synonyms
Beta-Defensin 16, DEFB-16, Beta 16, defensin, Beta-Defensin 116, Defensin, Beta 16, DEFB16.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.
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Background
Title: Beta Defensin 116 Human Recombinant: An Insight into its Antimicrobial Properties and Therapeutic Applications
Abstract:
Beta defensin 116 (BD116) is a key member of the beta defensin family, known for its potent antimicrobial activity against various pathogens. This research paper provides an in-depth analysis of human recombinant BD116, focusing on its production, characterization, and potential applications in antimicrobial therapy. The paper highlights the significance of BD116 in innate immunity and its role in combating microbial infections. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant BD116 in various infectious diseases. The information presented in this paper aims to enhance our understanding of human recombinant BD116 and its utility as a research tool and a potential antimicrobial agent.Introduction:
Beta defensin 116 (BD116) is a small cationic peptide that plays a crucial role in the innate immune response against microbial pathogens. Human recombinant BD116, produced through genetic engineering techniques, offers a valuable tool for studying its antimicrobial properties and exploring its therapeutic potential.Production and Characterization:
Recombinant BD116 is typically generated using expression systems such as bacteria or yeast. The protein is then purified and characterized to ensure its structural integrity and antimicrobial activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant BD116.Antimicrobial Properties:
BD116 exhibits broad-spectrum antimicrobial activity against bacteria, fungi, and viruses. It functions by disrupting the microbial cell membrane and interfering with essential cellular processes. Recombinant BD116 serves as a valuable tool for investigating the mechanisms underlying its antimicrobial action and exploring its potential as an antimicrobial agent.Therapeutic Implications:
The emergence of multidrug-resistant pathogens poses a significant challenge in the treatment of infectious diseases. Recombinant BD116 holds promise as an alternative therapeutic option due to its potent antimicrobial properties. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant BD116 in various infectious diseases, including bacterial skin infections and respiratory tract infections.Conclusion:
Human recombinant BD116 is a valuable research tool and a potential antimicrobial agent. Its production, characterization, and applications in antimicrobial therapy contribute to our understanding of innate immunity and the development of novel therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant BD116 offer promising prospects for combating multidrug-resistant pathogens and improving outcomes in infectious diseases.What is the molecular weight/Mw of DEFB116 Protein?
DEFB116 Protein has a total Mw of 11.5kDa.
What is the source or expression system of DEFB116 Protein?
Escherichia Coli.
What is the Purity of DEFB116 Protein?
DEFB116 Protein is >80% pure as determined by SDS-PAGE.
What is the Biological Activity of DEFB116 Protein?
The biological functionality of DEFB116 Protein will be determined in the future.
What is the amino acid sequence of DEFB116 Protein?
MGSSHHHHHH SSGLVPRGSH MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.
What applications can DEFB116 Protein be used in?
DEFB116 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for DEFB116 Protein?
The endotoxin level is minimal, DEFB116 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
BD 4 HumanDescription:
Beta Defensin-4 Human Recombinant
HBD-4, DEFB-4, HBD4, DEFB104B, Beta-defensin 4, BD-4.
Product # :
CYT-599Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Beta Defensin-4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 50 amino acids and having a molecular mass of 6 kDa. The BD-4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DEFB4 (1mg/ml) was lyophilized with 20mM sodium Phosphate buffer pH-7.4 and 130mM NaCl.
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 human monocytes using a concentration range of 0.1-50 ng/ml, corresponding to a specific activity of 20,000-10,000,000 units/mg.More Info
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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
HBD-4, DEFB-4, HBD4, DEFB104B, Beta-defensin 4, BD-4.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Beta Defensin-4 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-3 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-4 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
EFELDRICGY GTARCRKKCR SQEYRIGRCP NTYACCLRKW DESLLNRTKP.
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Background
Beta Defensin-4 Human Recombinant: Exploring the Potential of a Novel Antimicrobial Peptide
Abstract:
Beta Defensin-4 (hBD-4) human recombinant is a promising antimicrobial peptide with unique properties and potential therapeutic applications. This research paper provides an in-depth analysis of hBD-4, including its characteristics, mode of action, and potential uses. Furthermore, novel methodologies for the production and optimization of hBD-4 human recombinant are proposed, shedding light on its future implications in the field of infectious disease management.
Introduction:
In the face of increasing drug-resistant infections, alternative therapeutic strategies are crucial. Antimicrobial peptides, such as hBD-4, have gained attention due to their broad-spectrum activity against pathogens. This paper aims to explore the distinctive features of hBD-4 and propose innovative approaches for its production and optimization.
Characteristics and Mode of Action:
hBD-4 is a cationic peptide comprising 50 amino acids and is characterized by a unique structure that contributes to its antimicrobial properties. The mechanism of action involves the disruption of microbial membranes and subsequent cell death. Additionally, hBD-4 exhibits immunomodulatory effects, including the stimulation of chemotaxis and modulation of the inflammatory response.
Production of hBD-4 Human Recombinant:
Efficient production methodologies for hBD-4 human recombinant are essential for its therapeutic applications. Various expression systems, such as bacterial, yeast, and mammalian cell-based platforms, have been explored. Each system presents advantages and challenges, necessitating careful selection for high yields and protein quality. Optimization strategies, including codon optimization, fusion protein tags, and growth conditions, have been employed to enhance production efficiency. Purification techniques, such as chromatography and ultrafiltration, have been optimized to isolate high-quality hBD-4 recombinant.
Potential Applications:
hBD-4 human recombinant demonstrates potential therapeutic applications in combating drug-resistant pathogens. Its broad-spectrum antimicrobial activity against bacteria, viruses, and fungi positions it as a promising candidate for infectious disease management. Moreover, hBD-4 shows promise in wound healing and tissue regeneration due to its ability to promote angiogenesis and stimulate cell migration. Exploring its potential in combination with drug delivery systems for targeted therapy is an exciting avenue for future research.
Conclusion:
hBD-4 human recombinant represents a novel antimicrobial peptide with diverse potential applications. Optimizing production methodologies and elucidating its mechanisms of action will further enhance its clinical utility. With its broad-spectrum antimicrobial activity and potential implications in wound healing and targeted therapy, hBD-4 human recombinant holds promise as an innovative therapeutic agent.
What is the molecular weight/Mw of BD4 Protein?
BD4 Protein has a total Mw of 6kDa.
What is the source or expression system of BD4 Protein?
Escherichia Coli.
What is the Purity of BD4 Protein?
BD4 Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of BD4 Protein?
Determined by its ability to chemoattract human monocytes using a concentration range of 0.1-50 ng/ml, corresponding to a specific activity of 20,000-10,000,000 units/mg.
What is the amino acid sequence of BD4 Protein?
EFELDRICGY GTARCRKKCR SQEYRIGRCP NTYACCLRKW DESLLNRTKP.
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.
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Name :
SARS MERS RBDDescription:
SARS MERS Spike Receptor Binding Domain Recombinant
Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERS, MERSCoV RBD, MERS RBD, receptor binding domain, RBD, Spike RBD protein, Spike glycoprotein, S glycoprotein, E2, Peplomer protein
Product # :
SARS-054Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SARS MERS RBD Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 258 amino acids (358-606 aa) and having a molecular mass of 28.2kDa.SARS MERS RBD is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The SARS MERS RBD solution (0.5mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Since April 2012, cases of the Middle East Respiratory Syndrome Coronavirus (MERS-CoV) have been identified in various countries. Coronaviruses are the cause of the common cold, SARS (severe acute respiratory syndrome) and other severe illnesses with high mortality rates, all are classified into coronavirus family. MERS-CoV is a new type of SARS found in the coronavirus family causing severe pneumonia with sudden and serious respiratory illness with high mortality rates as well. Since January 27th 2015, the WHO has reported 956 human cases, including 351 deaths. More cases of the new coronavirus strain are expected. Like in other coronaviruses, large surface spike glycoprotein is a central structural protein of this virus; it is located above the virion surface to bind and enter into the target cell. Spike protein has 2 domains- S1 and S2. The S1 domain is responsible for cellular tropism and interaction with target cell, while the S2 domain is responsible for membrane fusion. The C-terminal of S1 domain contains a receptor binding domain, and is also a potential target for vaccine development and an antigen for diagnosis.
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Synonyms
Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERS, MERSCoV RBD, MERS RBD, receptor binding domain, RBD, Spike RBD protein, Spike glycoprotein, S glycoprotein, E2, Peplomer protein
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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
ADPSGVYSVS SFEAKPSGSV VEQAEGVECD FSPLLSGTPP QVYNFKRLVF TNCNYNLTKL LSLFSVNDFT CSQISPAAIA SNCYSSLILD YFSYPLSMKS DLSVSSAGPI SQFNYKQSFS NPTCLILATV PHNLTTITKP LKYSYINKCS RLLSDDRTEV PQLVNANQYS PCVSIVPSTV WEDGDYYRKQ LSPLEGGGWL VASGSTVAMT EQLQMGFGIT VQYGTDTNSV CPKLEFANDT KIASQLGNCV EYHHHHHH
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 :
AtosibanDescription:
Atosiban
Product # :
HOR-239Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- HPLC, MS
Description
Atosiban also called ADH (Anti-Diuretic Hormone) has a molecular formula of C43H67N11O12S2, 3-Mercaptopropionyl-D-Tyr(ET)-Ile-Thr-Asn-Cys-Pro-Orn-Gly-NH2 having a Mw of 994.2 Dalton.
Formulation
The Atosiban peptide was lyophilized with no additives.
Purity
Greater than 98.0% as determined by analysis by RP-HPLC.
HPLC, MS
More Info
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Introduction
Atosiban is the first oxytocin antagonist to be specifically developed for the treatment of preterm labor. Atosiban has a specific mode of action, inhibiting oxytocin-induced uterine contractions by blocking oxytocin receptors in the uterus. Extensive clinical investigations have shown Atosiban to be at least as effective as current tocolytic agents. In addition, due to its novel and specific mode of action, Atosiban has a markedly improved maternal side effects profile compared with conventional therapies.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Atosiban although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Atosiban 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 Atosiban in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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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
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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
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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.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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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.
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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.
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Amino Acid Sequence
QSINNPITCL TKGGVCWGPC TGGFRQIGTC GLPRVRCCKK K.
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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.
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Name :
Thymosin a1 humanDescription:
Thymosin a1 Acetate
Product # :
HOR-243Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Thymosin a1 acetate, also known as thymalfasin has immunoregulatory properties enhancing immune functions. Thymosin a1 has a molecular formula of C129H215N33O55 a.a. sequence of Ac-Ser-Asp-Ala-Ala-Val-Asp-Thr-Ser-Ser-Glu-Ile-Thr-Thr-Lys-Asp-Leu-Lys-Glu-Lys-Lys-Glu-Val-Val-Glu-Glu-Ala-Glu-Asn-OH and having a Mw of 3108.32 Dalton.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Thymalfasin is a synthetic analogue of thymosin-alpha-1, a 28-amino acid protein derived from the precursor protein prothymosin-alpha. Exhibiting a variety of immunoregulating properties, thymosin-alpha-1 induces differentiation of murine T-cell precursors and human thymocytes and the terminal differentiation of functionally immature cord blood lymphocytes and induces production of IL-2, high affinity IL-2 receptors, and B-cell growth factors by peripheral blood mononuclear cells. T-helper and cytotoxic/suppressor T-cell populations are targets of thymosin activity. Thymosin-alpha-1 has been shown to increase the efficiency of antigen presentation by macrophages and to be an endogenous modulator of alpha-thrombin activity.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Thymosin a1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thymalfasin 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 Thymosin a1 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 THYMOSIN-A1 HUMAN Protein?
THYMOSIN-A1 HUMAN Protein has a total Mw of 3.1kDa.
What is the Purity of THYMOSIN-A1 HUMAN Protein?
THYMOSIN-A1 HUMAN Protein is >99% pure as determined by SDS-PAGE.
What is the Biological Activity of THYMOSIN-A1 HUMAN Protein?
The biological functionality of THYMOSIN-A1 HUMAN Protein will be determined in the future.
What applications can THYMOSIN-A1 HUMAN Protein be used in?
THYMOSIN-A1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for THYMOSIN-A1 HUMAN Protein?
The endotoxin level is minimal, THYMOSIN-A1 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.
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Name :
S100A11 HumanDescription:
S100 Calcium Binding Protein A11 Human Recombinant
Protein S100-A11, S100 calcium-binding protein A11, Calgizzarin, MLN 70, S100A11, MLN70, S100C.
Product # :
PRO-385Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
S100A11 Human Recombinant is expressed in E. coli having a molecular weight of 17kDa fused to an amino terminal hexahistidine tag.
Source
Escherichia Coli.
Formulation
S100A11 is supplied in PBS and 50% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
2 bands on Western blot at 17 and 34 kDa, respectively representing monomeric and dimeric form.More Info
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Introduction
S100A11 is a member of the S100 family of proteins which contains two EF-hand calcium-binding motifs and is thought to be involved in the regulation of a number of cellular processes including cell cycle progression and differentiation. S100A11 may function in motility, invasion and tubulin polymerisation. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. Chromosomal rearrangements and altered expression of S100A11 have been implicated in tumor metastasis.
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Synonyms
Protein S100-A11, S100 calcium-binding protein A11, Calgizzarin, MLN 70, S100A11, MLN70, S100C.
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Stability
Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Applications
S100A11 can be used directly as a positive control in Western blotting, ELISA, immunoprecipitation and other immunological experiments.
The biological activity of this product has not yet been tested.
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 :
STX17 HumanDescription:
Syntaxin-17 Human Recombinant
Syntaxin 17
Product # :
PRO-1712Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
STX17 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (1-229) and having a molecular mass of 28.6kDa.STX17 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The STX17 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 30% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
STX17 is a member of to the syntaxin family and contains 1 t-SNARE coiled-coil homology domain. STX17 is involved in vesicle trafficking to lysosomes and takes part in procedures associated with cell division.
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Synonyms
Syntaxin 17
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSEDEEK VKLRRLEPAI QKFIKIVIPT DLERLRKHQI NIEKYQRCRI WDKLHEEHIN AGRTVQQLRS NIREIEKLCL KVRKDDLVLL KRMIDPVKEE ASAATAEFLQ LHLESVEELK KQFNDEETLL QPPLTRSMTV GGAFHTTEAE ASSQSLTQIY ALPEIPQDQN AAESWETLEA DLIELSQLVT DFSLLVNSQQ EKIDSIADHV NSAAVNVEEG TKNLGKAAKY KL
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.